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Information on EC 7.4.2.6 - ABC-type oligopeptide transporter
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EC Tree
7.4.2.6 ABC-type oligopeptide transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of oligopeptides of varying nature. The binding protein determines the specificity of the system. cf. EC 7.4.2.9, ABC-type dipeptide transporter.
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Word Map
- 7.4.2.6
- dipeptide
- tripeptides
-
importins
-
proton-coupled
-
cargo
-
caco-2
-
prodrugs
-
hpept1
-
nucleocytoplasmic
-
glycylsarcosine
-
peptidomimetic
-
proton-dependent
-
gly-sar
- nucleoporins
- cephalexin
-
carrier-mediated
-
rangtp
-
peptide-like
-
pept1-mediated
-
slc15a1
-
karyopherins
-
importin-beta
- bestatin
-
ergic-53
- acyclovir
- cefadroxil
- ntf2
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
+
=
+
+
+
+
+
oligopeptide-[oligopeptide-binding protein][side 1]
=
+
+
oligopeptide[side 2]
+
[oligopeptide-binding protein][side 1]
Synonyms
oligopeptide transporter, transport receptor, oligopeptide permease, glutathione transporter, oligopeptide-binding protein, atopt6, oligopeptide transporter 1, scopt1, oligopeptide permease a, oligopeptide-binding protein a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BldK transporter
EC 3.6.3.23
-
-
formerly
-
oligogopeptide permease
oligogopeptide permease protein A
oligopeptide ABC transporter
oligopeptide permease
oligopeptide permease A
oligopeptide transporter
oligopeptide-binding protein
oligopeptide-transporting ATPase
-
-
-
-
Opp
Opp1
Opp3
OppA
OppF
PepT1
additional information
oligopeptide permease
-
-
-
-
Opp
the Opp system consists of five oligopeptide-binding proteins (OppA1 to OppA5), two heterodimeric cytoplasmic membrane permeases (OppB1C1 and OppB2C2), and a nucleotide-binding domain heterodimer (OppDF) that drives transport by hydrolyzing ATP
Opp
the Opp system consists of five oligopeptide-binding proteins (OppA1 to OppA5), two heterodimeric cytoplasmic membrane permeases (OppB1C1 and OppB2C2), and a nucleotide-binding domain heterodimer (OppDF) that drives transport by hydrolyzing ATP
-
OppA
-
the surface-localised substrate-binding domain OppA of the oligopeptide permease
additional information
-
AppA, OppA, and Dpp belong to the ATP-binding casette family, the ABC-type ATPases
additional information
the enzyme belongs to the oligopeptide transporters of the OPT family
additional information
-
Opt2 is a member of the oligopeptide transporter family
additional information
-
Opp enzymes belong to the ATP-binding casette family, the ABC-type ATPases
additional information
-
peptide transport systems involved in the signaling pathways belong to the superfamily of ATP-binding cassette, ABC, transporters composed of five protein subunits
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1] = ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric acid anhydride
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, oligopeptide-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of oligopeptides of varying nature. The binding protein determines the specificity of the system. cf. EC 7.4.2.9, ABC-type dipeptide transporter.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + AtCLE19p12/out
ADP + phosphate + AtCLE19p12/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + CLE/out
ADP + phosphate + CLE/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA, CLE is transported by AtOPT6 with high affinity
-
-
?
ATP + H2O + GGFM/out
ADP + phosphate + GGFM/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + GGGQATGPPNTSYMPGMPGD-[GGGQATGPPNTSYMPGMPGD-binding protein][side 1]
ADP + phosphate + GGGQATGPPNTSYMPGMPGD[side 2] + [GGGQATGPPNTSYMPGMPGD-binding protein][side 1]
ATP + H2O + GSSG/out
ADP + phosphate + GSSG/in
-
in Xenopus laevis oocytes, injected with ScOPT1 cRNA
-
-
?
ATP + H2O + KLG/out
ADP + phosphate + KLG/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + KLGL/out
ADP + phosphate + KLGL/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + KLLLG/out
ADP + phosphate + KLLLG/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + KLLLLG/out
ADP + phosphate + KLLLLG/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
ATP + H2O + phosphinotricyl-alanyl-alanine/out
ADP + phosphate + phosphinotricyl-alanyl-alanine/in
ATP + H2O + X-Ala-Ala-Ala-[X-Ala-Ala-Ala-binding protein][side 1]
ADP + phosphate + X-Ala-Ala-Ala[side 2] + [X-Ala-Ala-Ala-binding protein][side 1]
ATP + H2O + bradykinin/out
ADP + phosphate + bradykinin/in
i.e. RPPGFSPFR, specific for isozyme OppA2
-
-
?
ATP + H2O + bradykinin/out
ADP + phosphate + bradykinin/in
i.e. RPPGFSPFR, specific for isozyme OppA2, ATP hydrolysis is coupled to peptide translocation
-
-
?
ATP + H2O + GGFL/out
ADP + phosphate + GGFL/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA. GGFL-induced currents are pH-dependent
-
-
?
ATP + H2O + GGFL/out
ADP + phosphate + GGFL/in
-
in Xenopus laevis oocytes, injected with ScOPT1 cRNA
-
-
?
ATP + H2O + GGGQATGPPNTSYMPGMPGD-[GGGQATGPPNTSYMPGMPGD-binding protein][side 1]
ADP + phosphate + GGGQATGPPNTSYMPGMPGD[side 2] + [GGGQATGPPNTSYMPGMPGD-binding protein][side 1]
-
-
-
?
ATP + H2O + GGGQATGPPNTSYMPGMPGD-[GGGQATGPPNTSYMPGMPGD-binding protein][side 1]
ADP + phosphate + GGGQATGPPNTSYMPGMPGD[side 2] + [GGGQATGPPNTSYMPGMPGD-binding protein][side 1]
-
-
-
?
ATP + H2O + GSH/out
ADP + phosphate + GSH/in
-
in Xenopus laevis oocytes, injected with AtOPT6 cRNA. GSH-induced currents are pH-dependent, low affinity GSH transport of AtOPT6
-
-
?
ATP + H2O + GSH/out
ADP + phosphate + GSH/in
-
in Xenopus laevis oocytes, injected with ScOPT1 cRNA
-
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme is required for expression of the srf operon in response to changes in culture pH
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme imports exogenous peptides that play roles as source of amino acids and in the signalling pathways leading to development of competence and sporulation, overview
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
ATP hydrolysis is coupled to peptide translocation, the enzyme has a lipid-modified, membrane-anchored extracellular protein binding domain which serve as a receptor for the system, peptide ligand pocket structure of AppA, overview
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
transport of the phytotoxic tripeptide phaseolotoxin into E. coli cells or cells of Salmonella typhimurium. Mutants defective in oligopeptide permease are resistant to phaseolotoxin
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the genes of the trp-linked opp operon are subject to transcriptional regulation, their expression is elevated by supplementation of the growth medium with either L-Leu or L-Ala and by growth of the opp-lac fusion-containing strains under anaerobic conditions
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
growth of E. coli in the presence of Leu results in increased synthesis of the OppA-encoded periplasmic binding protein
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
transport of the phytotoxic tripeptide phaseolotoxin into E. coli cells or cells of Salmonella typhimurium. Mutants defective in oligopeptide permease are resistant to phaseolotoxin
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
enzyme plays an important nutritional role and is required for the recycling of cell wall peptides
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the Ami transporter is involved in the regulatory pathway that controls the induction of the competence state in Streptococcus thermophilus, and also that natural transformation can be turned on in CDM during the exponential growth phase, oligopeptide-binding protein AmiA3 plays the major role, overview
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme is responsible for the import of an extracellular signal governing aerial mycelium formation
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the extracytoplasmic lipid-anchored substrate-binding protein, or receptor, OppA delivers peptides to an integral membrane complex OppBCDF, or translocator, where, on ATP binding and hydrolysis, translocation across the membrane takes place, mechanism studied in model membrane vesicles, overview
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme binds peptides of 3 to 16 amino acids, regardless of the presence of arginine in the peptide
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme binds peptides of 3 to 16 amino acids, regardless of the presence of arginine in the peptide
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
oligopeptides internalized by oligopeptide permease transporters play key roles in bacterial nutrition, signaling, and virulence, opp-3 is the only transporter to be regulated by specific amino acids, tyrosine and phenylalanine at the transcription level, and Opp-3 appears to be the main Opp system supplying the cell with peptides as nutritional sources, overview
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
Hly-OppA has multiple functions in solute binding, in in vitro hemolysis, in antibiotic resistance, and as a virulence factor in bacterial pathogenesis, overview
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the oligopeptide-binding protein, OppA, binds and ushers oligopeptide substrates to the membrane-associated oligopeptide permease, Opp, a multi-component ABC-type transporter involved in the uptake of oligopeptides
-
-
?
ATP + H2O + phosphinotricyl-alanyl-alanine/out
ADP + phosphate + phosphinotricyl-alanyl-alanine/in
import of the toxic tripeptide, isozymes OppA1 and OppA2
-
-
?
ATP + H2O + phosphinotricyl-alanyl-alanine/out
ADP + phosphate + phosphinotricyl-alanyl-alanine/in
a toxic tripeptide, isozymes OppA1 and OppA2, ATP hydrolysis is coupled to peptide translocation
-
-
?
ATP + H2O + phytochelatin/out
ADP + phosphate + phytochelatin/in
-
i.e. (gamma -Glu-Cys) 2 -Gly, in Xenopus laevis oocytes, injected with AtOPT6 cRNA
-
-
?
ATP + H2O + phytochelatin/out
ADP + phosphate + phytochelatin/in
-
i.e. (gamma -Glu-Cys) 2 -Gly, in Xenopus laevis oocytes, injected with ScOPT1 cRNA
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
-
?
ATP + H2O + X-Ala-Ala-Ala-[X-Ala-Ala-Ala-binding protein][side 1]
ADP + phosphate + X-Ala-Ala-Ala[side 2] + [X-Ala-Ala-Ala-binding protein][side 1]
-
-
-
?
ATP + H2O + X-Ala-Ala-Ala-[X-Ala-Ala-Ala-binding protein][side 1]
ADP + phosphate + X-Ala-Ala-Ala[side 2] + [X-Ala-Ala-Ala-binding protein][side 1]
-
-
-
?
additional information
?
-
-
AtOPT6 displays high affinity for penta- and dodecapeptides, but low affinity for GSH, substrate specificity of AtOPT6, inward currents caused by KLLG and KLLLG application are 3 to 7fold greater than with KLG, overview
-
-
?
additional information
?
-
-
enzyme stimulates competence development and the initiation of sporulation by importing specific signaling peptides
-
-
?
additional information
?
-
-
substrate binding proteins OppA1, OppA2 show preference for tripeptides over dipeptides and loger-chain peptides. OppA1 is able to accomodate peptides composed of bulky residues, OppA2 and OppA3 prefer peptides composed of small nonpolar amino acids. All three Opp proteins prefer L-amino acids rather than D-amino acids
-
-
?
additional information
?
-
-
the Borrelia burgdorferi oligopeptide permease contains five different substrate binding proteins, i.e. OppA proteins, that interact with the integral membrane components of the transporter, expression of the OppA proteins is individually regulated and may play different roles in adaptation to host environments, overview
-
-
?
additional information
?
-
-
the Borrelia burgdorferi oligopeptide permease contains five different substrate binding proteins, i.e. OppA proteins, that interact with the integral membrane components of the transporter, expression of the OppA proteins is individually regulated and may play different roles in adaptation to host environments, overview
-
-
?
additional information
?
-
-
OppA protein does not play a direct role in the sensitivity to aminoglycosides in Escherichia coli K12, overview
-
-
?
additional information
?
-
-
OppA protein does not play a direct role in the sensitivity to aminoglycosides in Escherichia coli K12, overview
-
-
?
additional information
?
-
PepT1 may play an important role in the larval nutrition since it is widely expressed in the digestive tract, PepT1 expression depends on the diet, overview
-
-
?
additional information
?
-
-
PepT1 may play an important role in the larval nutrition since it is widely expressed in the digestive tract, PepT1 expression depends on the diet, overview
-
-
?
additional information
?
-
-
the enzyme follows a mechanism for peptide selection based on amino-acid composition rather than sequence, overview
-
-
?
additional information
?
-
-
OppA binds peptides of an exceptionally wide range of lengths of 4 to 35 residues with no apparent sequence preference. A huge cavity allows binding of very long peptides, and a lack of constraints for the position of the N and C termini of the ligand is compatible with binding of peptides with varying lengths, e.g. bradykinin, RPPGFSPFR
-
-
?
additional information
?
-
-
the enzyme does not have a specific affinity for peptides containing arginine
-
-
?
additional information
?
-
-
the enzyme does not have a specific affinity for peptides containing arginine
-
-
?
additional information
?
-
-
the ecto-ATPase OppA, the surface-localized substrate-binding domain of the oligopeptide permease, of Mycoplasma hominis induces ATP release and both apoptotic and necrotic cell death in HeLa cells, overview
-
-
?
additional information
?
-
-
ScOPT1 substrate specificity, overview. KLLLG, RPPGF, DRVYIHPF or AtCLE19p12 cause no inward currents in ScOPT1-expressing oocytes
-
-
?
additional information
?
-
-
opp3 participates in extracellular protease regulation during growth in milk
-
-
?
additional information
?
-
-
opp3 participates in extracellular protease regulation during growth in milk
-
-
?
additional information
?
-
-
OppA is important in pathogenesis of group A streptococci
-
-
?
additional information
?
-
-
the oligopeptide transport system is essential for the development of natural competence in Streptococcus thermophilus strain LMD-9, mutational analysis, overview
-
-
?
additional information
?
-
the two isozymes OppA1 and OppA2 are essential for production of beta-lactamase inhibitor clavulinic acid
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
the purified protein exhibits host-specific in vitro hemolytic activity against various mammalian erythrocytes and apparent cytotoxicity in CHO-K1 cells
-
-
?
additional information
?
-
-
the purified protein exhibits host-specific in vitro hemolytic activity against various mammalian erythrocytes and apparent cytotoxicity in CHO-K1 cells
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + bradykinin/out
ADP + phosphate + bradykinin/in
i.e. RPPGFSPFR, specific for isozyme OppA2
-
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
ATP + H2O + phosphinotricyl-alanyl-alanine/out
ADP + phosphate + phosphinotricyl-alanyl-alanine/in
import of the toxic tripeptide, isozymes OppA1 and OppA2
-
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme is required for expression of the srf operon in response to changes in culture pH
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme imports exogenous peptides that play roles as source of amino acids and in the signalling pathways leading to development of competence and sporulation, overview
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
transport of the phytotoxic tripeptide phaseolotoxin into E. coli cells or cells of Salmonella typhimurium. Mutants defective in oligopeptide permease are resistant to phaseolotoxin
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the genes of the trp-linked opp operon are subject to transcriptional regulation, their expression is elevated by supplementation of the growth medium with either L-Leu or L-Ala and by growth of the opp-lac fusion-containing strains under anaerobic conditions
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
growth of E. coli in the presence of Leu results in increased synthesis of the OppA-encoded periplasmic binding protein
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
transport of the phytotoxic tripeptide phaseolotoxin into E. coli cells or cells of Salmonella typhimurium. Mutants defective in oligopeptide permease are resistant to phaseolotoxin
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
enzyme plays an important nutritional role and is required for the recycling of cell wall peptides
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the Ami transporter is involved in the regulatory pathway that controls the induction of the competence state in Streptococcus thermophilus, and also that natural transformation can be turned on in CDM during the exponential growth phase, oligopeptide-binding protein AmiA3 plays the major role, overview
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme is responsible for the import of an extracellular signal governing aerial mycelium formation
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
-
a 655 Da oligopeptide
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the extracytoplasmic lipid-anchored substrate-binding protein, or receptor, OppA delivers peptides to an integral membrane complex OppBCDF, or translocator, where, on ATP binding and hydrolysis, translocation across the membrane takes place, mechanism studied in model membrane vesicles, overview
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme binds peptides of 3 to 16 amino acids, regardless of the presence of arginine in the peptide
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the enzyme binds peptides of 3 to 16 amino acids, regardless of the presence of arginine in the peptide
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
oligopeptides internalized by oligopeptide permease transporters play key roles in bacterial nutrition, signaling, and virulence, opp-3 is the only transporter to be regulated by specific amino acids, tyrosine and phenylalanine at the transcription level, and Opp-3 appears to be the main Opp system supplying the cell with peptides as nutritional sources, overview
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
-
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
Hly-OppA has multiple functions in solute binding, in in vitro hemolysis, in antibiotic resistance, and as a virulence factor in bacterial pathogenesis, overview
-
-
?
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
-
the oligopeptide-binding protein, OppA, binds and ushers oligopeptide substrates to the membrane-associated oligopeptide permease, Opp, a multi-component ABC-type transporter involved in the uptake of oligopeptides
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
-
?
additional information
?
-
-
enzyme stimulates competence development and the initiation of sporulation by importing specific signaling peptides
-
-
?
additional information
?
-
-
the Borrelia burgdorferi oligopeptide permease contains five different substrate binding proteins, i.e. OppA proteins, that interact with the integral membrane components of the transporter, expression of the OppA proteins is individually regulated and may play different roles in adaptation to host environments, overview
-
-
?
additional information
?
-
-
the Borrelia burgdorferi oligopeptide permease contains five different substrate binding proteins, i.e. OppA proteins, that interact with the integral membrane components of the transporter, expression of the OppA proteins is individually regulated and may play different roles in adaptation to host environments, overview
-
-
?
additional information
?
-
-
OppA protein does not play a direct role in the sensitivity to aminoglycosides in Escherichia coli K12, overview
-
-
?
additional information
?
-
-
OppA protein does not play a direct role in the sensitivity to aminoglycosides in Escherichia coli K12, overview
-
-
?
additional information
?
-
PepT1 may play an important role in the larval nutrition since it is widely expressed in the digestive tract, PepT1 expression depends on the diet, overview
-
-
?
additional information
?
-
-
PepT1 may play an important role in the larval nutrition since it is widely expressed in the digestive tract, PepT1 expression depends on the diet, overview
-
-
?
additional information
?
-
-
the enzyme follows a mechanism for peptide selection based on amino-acid composition rather than sequence, overview
-
-
?
additional information
?
-
-
the ecto-ATPase OppA, the surface-localized substrate-binding domain of the oligopeptide permease, of Mycoplasma hominis induces ATP release and both apoptotic and necrotic cell death in HeLa cells, overview
-
-
?
additional information
?
-
-
opp3 participates in extracellular protease regulation during growth in milk
-
-
?
additional information
?
-
-
opp3 participates in extracellular protease regulation during growth in milk
-
-
?
additional information
?
-
-
OppA is important in pathogenesis of group A streptococci
-
-
?
additional information
?
-
-
the oligopeptide transport system is essential for the development of natural competence in Streptococcus thermophilus strain LMD-9, mutational analysis, overview
-
-
?
additional information
?
-
the two isozymes OppA1 and OppA2 are essential for production of beta-lactamase inhibitor clavulinic acid
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
-
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
Vibrio fluvialis KCTC 2473 / ATCC 33809
isozyme OppA is involved in biofilm formation in Vibrio fluvialis
-
-
?
additional information
?
-
the purified protein exhibits host-specific in vitro hemolytic activity against various mammalian erythrocytes and apparent cytotoxicity in CHO-K1 cells
-
-
?
additional information
?
-
-
the purified protein exhibits host-specific in vitro hemolytic activity against various mammalian erythrocytes and apparent cytotoxicity in CHO-K1 cells
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4',4'-diisothiocyanostylbene-2',2'-disulfonic acid
-
0.5 mM, about 25% residual activity
Trypsin
-
tryptic digestion of OppA was protected by ATP and ADP but not by GTP or CTP
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
microcin J25
-
the ATPase activity of the enzyme reconstituted in proteoliposomes is stimulated by microcin J25 in a concentration-dependent manner
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Targeted delivery to PEPT1-overexpressing cells: acidic, basic, and secondary floxuridine amino acid ester prodrugs.
Alzheimer Disease
[Effect of electroacupuncture stimulation of "Baihui" (GV 20) and " Yongquan" (KI 1) on expression of hippocampal amyloid-? and low density lipoprotein receptor-related protein-1 in APP/PS 1 transgenic mice].
Anemia
Double knockout Nme1/Nme2 mouse model suggests a critical role for NDP kinases in erythroid development.
Breast Neoplasms
Nuclear transport receptor karyopherin-?2 promotes malignant breast cancer phenotypes in vitro.
Carcinoma
An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2.
Carcinoma
KPNB1 Inhibitor Importazole Reduces Ionizing Radiation-Increased Cell Surface PD-L1 Expression by Modulating Expression and Nuclear Import of IRF1.
Carcinoma, Hepatocellular
Enhanced delivery of drugs to the liver by adenovirus-mediated heterologous expression of the human oligopeptide transporter PEPT1.
Carcinoma, Squamous Cell
KPNB1 Inhibitor Importazole Reduces Ionizing Radiation-Increased Cell Surface PD-L1 Expression by Modulating Expression and Nuclear Import of IRF1.
Colitis
SLC15A4 mediates M1-prone metabolic shifts in macrophages and guards immune cells from metabolic stress.
Colitis, Ulcerative
Peptide Receptor-Targeted Fluorescent Probe: Visualization and Discrimination between Chronic and Acute Ulcerative Colitis.
Cystic Fibrosis
Lubiprostone: evaluation of the newest medication for the treatment of adult women with constipation-predominant irritable bowel syndrome.
Dengue
A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-beta and the viral helicase, NS3.
Essential Hypertension
Erythrocytic cation transport receptor numbers and activity in pregnancies complicated by essential hypertension and pre-eclampsia.
Hepatitis C
The core protein of hepatitis C virus is imported into the nucleus by transport receptor Kap123p but inhibits Kap121p-dependent nuclear import of yeast AP1-like transcription factor in yeast cells.
Herpesviridae Infections
Interactions of the dipeptide ester prodrugs of acyclovir with the intestinal oligopeptide transporter: competitive inhibition of glycylsarcosine transport in human intestinal cell line-Caco-2.
Hypersensitivity
Reverse genetic analysis of the glutathione metabolic pathway suggests a novel role of PHGPX and URE2 genes in aluminum resistance in Saccharomyces cerevisiae.
Hyperthyroidism
Decreased activity and expression of intestinal oligopeptide transporter PEPT1 in rats with hyperthyroidism in vivo.
Infections
Identification of Mycobacterium avium genes expressed during in vivo infection and the role of the oligopeptide transporter OppA in virulence.
Inflammatory Bowel Diseases
Chemical Modulation of the Human Oligopeptide Transporter 1, hPepT1.
Inflammatory Bowel Diseases
Lactobacillus plantarum Consumption Increases PepT1-Mediated Amino Acid Absorption by Enhancing Protein Kinase C Activity in Spontaneously Colitic Mice.
Inflammatory Bowel Diseases
PepT1 oligopeptide transporter (SLC15A1) gene polymorphism in inflammatory bowel disease.
Influenza, Human
Effect of milk on the pharmacokinetics of oseltamivir in healthy volunteers.
Lyme Disease
Oligopeptide permease in Borrelia burgdorferi: putative peptide-binding components encoded by both chromosomal and plasmid loci.
Lyme Disease
The oligopeptide ABC transporter OppA4 negatively regulates the virulence factor OspC production of the Lyme disease pathogen.
Meningitis, Pneumococcal
In vivo proteomics identifies the competence regulon and AliB oligopeptide transporter as pathogenic factors in pneumococcal meningitis.
Neoplasms
Boron delivery for boron neutron capture therapy targeting a cancer-upregulated oligopeptide transporter.
Neoplasms
Importin-?/karyopherin-?1 modulates mitotic microtubule function and taxane sensitivity in cancer cells via its nucleoporin-binding region.
Neoplasms
IPO5 promotes the proliferation and tumourigenicity of colorectal cancer cells by mediating RASAL2 nuclear transportation.
Neoplasms
Nuclear transport of Ras-associated tumor suppressor proteins: different transport receptor binding specificities for arginine-rich nuclear targeting signals.
Neoplasms
Subcellular Fractionation of Primary Chronic Lymphocytic Leukemia Cells to Monitor Nuclear/Cytoplasmic Protein Trafficking.
Neoplasms
Targeted delivery to PEPT1-overexpressing cells: acidic, basic, and secondary floxuridine amino acid ester prodrugs.
Neoplasms
The nuclear transport receptor Importin-11 is a tumor suppressor that maintains PTEN protein.
Neurofibrosarcoma
EZH2-miR-30d-KPNB1 pathway regulates malignant peripheral nerve sheath tumour cell survival and tumourigenesis.
Otitis
Stringently Defined Otitis Prone Children Demonstrate Deficient Naturally Induced Mucosal Antibody Response to Moraxella catarrhalis Proteins.
Pancreatic Neoplasms
Inhibition of oligopeptide transporter suppress growth of human pancreatic cancer cells.
Pancreatic Neoplasms
KPNA7, a nuclear transport receptor, promotes malignant properties of pancreatic cancer cells in vitro.
Pre-Eclampsia
Erythrocytic cation transport receptor numbers and activity in pregnancies complicated by essential hypertension and pre-eclampsia.
Prostatic Hyperplasia
Expression of proton-coupled oligopeptide transporter (POTs) in prostate of mice and patients with benign prostatic hyperplasia (BPH) and prostate cancer (PCa).
Prostatic Neoplasms
Expression of proton-coupled oligopeptide transporter (POTs) in prostate of mice and patients with benign prostatic hyperplasia (BPH) and prostate cancer (PCa).
Streptococcal Infections
Effects of oligopeptide permease in group a streptococcal infection.
Tuberculosis
A peptide permease mutant of Mycobacterium bovis BCG resistant to the toxic peptides glutathione and S-nitrosoglutathione.
Tuberculosis
An oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages.
Tuberculosis
Evaluation of the immunogenicity of pBudCE4.1 plasmids encoding mycolyl-transferase Ag85A and phosphate transport receptor PstS-3 from Mycobacterium tuberculosis.
Tuberculosis
Immunogenicity and protective efficacy of tuberculosis DNA vaccines combining mycolyl-transferase Ag85A and phosphate transport receptor PstS-3.
Tuberculosis
Induction of in vivo functional Db-restricted cytolytic T cell activity against a putative phosphate transport receptor of Mycobacterium tuberculosis.
Tuberculosis
Mycobacterium tuberculosis modulates its cell surface via an oligopeptide permease (Opp) transport system.
Virus Diseases
Pharmacokinetic studies and LC-MS/MS method development of ganciclovir and dipeptide monoester prodrugs in Sprague Dawley rats.
Virus Diseases
Pharmacokinetics of novel dipeptide ester prodrugs of acyclovir after oral administration: intestinal absorption and liver metabolism.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
PepT1 shows an increase in apparent substrate affinity at acidic pH, kinetics at pH 6.0-8.0, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0395
adenosine 5'-(beta,gamma-imido)triphosphate
Escherichia coli
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
substrate specificity and current kinetics, overview
additional information
biofilm formation assay of wild-type and mutant strains
additional information
-
biofilm formation assay of wild-type and mutant strains
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
PepT1 activity is pH-dependent and shows an increase in apparent substrate affinity at acidic pH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
group A streptococci, i.e. GAS, strains SW507 and A-20, genes oppA, oppB, oppC, oppD, and oppF, encoding isozymes OppA, OppB, OppC, OppD, and OppF
-
-
brenda
ami genes encoded peptide transporter system, strains LMD-9, GCNRZ1066, and LMG18311 posessing two or three oligopeptide-binding proteins
-
-
brenda
orf7, isozyme oppA1; ATCC 24076, genes oppA1 and oppA2
SwissProt
brenda
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
-
-
brenda
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
-
-
brenda
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
-
-
brenda
Vibrio fluvialis KCTC 2473 / ATCC 33809
strains NCTC8325 and RN6390, four opp operons, opp-1, opp-2, opp-3, and opp-4, plus an opp-5A gene encoding a putative peptide-binding protein
-
-
brenda
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
-
-
brenda
OppA; opp gene cluster encoding five isozymes including OppA
SwissProt
brenda
OppB; opp gene cluster encoding five isozymes including OppB
SwissProt
brenda
OppC; opp gene cluster encoding five isozymes including OppC
SwissProt
brenda
OppD; opp gene cluster encoding five isozymes including OppD
SwissProt
brenda
OppF; opp gene cluster encoding five isozymes including OppF
SwissProt
brenda
Vibrio fluvialis KCTC 2473 / ATCC 33809
OppA; opp gene cluster encoding five isozymes including OppA
SwissProt
brenda
Vibrio fluvialis KCTC 2473 / ATCC 33809
OppB; opp gene cluster encoding five isozymes including OppB
SwissProt
brenda
Vibrio fluvialis KCTC 2473 / ATCC 33809
OppC; opp gene cluster encoding five isozymes including OppC
SwissProt
brenda
Vibrio fluvialis KCTC 2473 / ATCC 33809
OppD; opp gene cluster encoding five isozymes including OppD
SwissProt
brenda
Vibrio fluvialis KCTC 2473 / ATCC 33809
OppF; opp gene cluster encoding five isozymes including OppF
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PepT1 is expressed in the epithelium throughout the digestive system except the esophagus and sphincter regions
brenda
expression of PepT1 increases during development when the larvae are feeded with zooplankton instead of rotifers
brenda
additional information
additional information
-
no expression of OPTs in in the root epidermis or root hair cells
brenda
additional information
-
growth and virulence assessment in mice
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
substrate binding protein OppA of the permease complex
brenda
-
more than 80% of the surface-localised ATPase activity of Mycoplasma hominis is derived from OppA, implicating that OppA is the main ATPase on the surface of mycoplasma cells
brenda
-
the extracytoplasmic lipid-anchored substrate-binding protein, or receptor, OppA delivers peptides to an integral membrane complex OppBCDF, or translocator, where, on ATP binding and hydrolysis, translocation across the membrane takes place
brenda
-
OppB, OppC and OppD are membrane-associated proteins
brenda
-
OppB and OppC are highly hydrophobic, integral membrane proteins. Each of these two proteins spans the membrane six times, with the N-terminus and the C-terminus both being located at the cytoplasmic face of the membrane
brenda
-
OppF, a component of the oligopeptide permease is a peripheral membrane protein located on the cytoplasmic side of the inner membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
aknockout mutant shows marked impairment in its capacity to persist in the respiratory tract compared to the wild type in a mouse pulmonary clearance model
malfunction
-
mutations in OppA transport domain result in Mycobacterium avium impairment in macrophages and in mice
malfunction
loss of enzyme function abrogates spirochete growth in vitro
malfunction
-
aknockout mutant shows marked impairment in its capacity to persist in the respiratory tract compared to the wild type in a mouse pulmonary clearance model
-
malfunction
-
loss of enzyme function abrogates spirochete growth in vitro
-
physiological function
CgOPT1 is involved in regulation of fungal response to iodoacetic acid, and is also necessary for full virulence, but it is unclear whether this phenotype is related to auxin. CgOpt1 is probably associated only with light-dependent sporulation, and is not required for light-independent sporulation
physiological function
-
PepT1 is an integral plasma membrane protein responsible for the uptake of dietary di- and tripeptides in cells. It transports peptides against a concentration gradient in a pH-dependent manner. PepT1 transporter is electrogenic
physiological function
-
ScOPT1 is a high affinity GSH transporter. Fungal OPTs function in nutrient uptake from the environment
physiological function
-
the bacterium controls production of some exposed molecules by importing oligopeptide signals via permeases. Such oligopeptides modulate intracellular signaling pathways, overview. Also Opp is required to modulate the expression of several genes, most of them encoding surface-exposed molecules, e.g. the virulence-associated lipids mycolic acids and phthiocerol dimycocerosates, as well as PE-family proteins
physiological function
-
unlike in fungi, plant OPTs do not function in nutrient uptake from the environment, but OPT6 can transport plant signaling peptides
physiological function
-
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette transporter, shows direct involvement in the extracellular signaling
physiological function
-
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette transporter, shows direct involvement in the extracellular signaling
physiological function
-
the enzyme confers specific resistance to taurine-conjugated bile salts. Enzyme overexpression confers 20fold higher tolerance to 0.5% oxgall in Lactobacillus salivarius as well as 1.8fold and 3.6fold higher survival when exposed to the sublethal concentration of sodium taurocholate and sodium taurodeoxycholate, respectively, while no significant change is observed when exposed to sodium glycocholate and sodium glycodeoxycholate. In addition, enzyme overexpression also leads to significantly increased resistance to heat (55°C) and salt (7.5% (w/v) NaCl) stresses
physiological function
-
the enzyme is involved in an active transport of oligopeptides across the cell membrane
physiological function
the enzyme is essential for viability, morphogenesis, and virulence within the mammalian host
physiological function
-
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette transporter, shows direct involvement in the extracellular signaling
-
physiological function
-
the enzyme is essential for viability, morphogenesis, and virulence within the mammalian host
-
physiological function
-
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette transporter, shows direct involvement in the extracellular signaling
-
additional information
-
Genes Mtb Rv3666c-Rv3663c encode an Opp transport system dispensable for in vitro growth. The Opp loss of function mutant shows no in vitro growth defect, but has diminished burden during chronic infection and produces a slightly delayed time to death of animals when compared to wild-type infection. But disruption of the opp locus affects the expression of genes involved in the production of mycobacterial lipids
additional information
morphology of wild type and cgopt1 mutants in presence or absence of iodoacetic acid, overview
additional information
-
transcription of the bldK-g operon is affected by adpA deletion, but appears not to be directly regulated by AdpA
additional information
-
transcription of the bldK-g operon is affected by adpA deletion, but appears not to be directly regulated by AdpA
additional information
-
transcription of the bldK-g operon is affected by adpA deletion, but appears not to be directly regulated by AdpA
-
additional information
-
transcription of the bldK-g operon is affected by adpA deletion, but appears not to be directly regulated by AdpA
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ABCB9_HUMAN
766
7
84475
Swiss-Prot
Secretory Pathway (Reliability: 1)
ABCB9_MOUSE
762
7
83963
Swiss-Prot
Secretory Pathway (Reliability: 1)
ABCB9_RAT
762
7
84033
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q0KC28_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
320
0
34425
TrEMBL
-
Q0KBL6_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
337
0
35805
TrEMBL
-
Q0K6K3_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
353
0
38948
TrEMBL
-
Q88PG6_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
530
0
59564
TrEMBL
-
Q88PH2_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
322
0
35754
TrEMBL
-
G7LIW2_MEDTR
285
0
31365
TrEMBL
Chloroplast (Reliability: 4)
F8GM33_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
330
0
36344
TrEMBL
-
D2BLF7_LACLK
Lactococcus lactis subsp. lactis (strain KF147)
319
0
35975
TrEMBL
-
G8Q7A4_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
285
5
30602
TrEMBL
-
Q0K7J3_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
348
0
37579
TrEMBL
-
Q0K259_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
330
0
36317
TrEMBL
-
Q88PH1_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
322
0
34915
TrEMBL
-
D5APA1_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
341
0
37140
TrEMBL
-
G4L2W5_TETHN
Tetragenococcus halophilus (strain DSM 20338 / JCM 20259 / NCIMB 9735 / NBRC 12172)
319
0
36033
TrEMBL
-
Q0K7J2_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
321
0
34078
TrEMBL
-
K4LES9_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)
332
0
36133
TrEMBL
-
Q88PG5_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
541
0
60367
TrEMBL
-
G4L2W6_TETHN
Tetragenococcus halophilus (strain DSM 20338 / JCM 20259 / NCIMB 9735 / NBRC 12172)
352
0
39258
TrEMBL
-
Q0K258_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
351
0
38425
TrEMBL
-
Q0K3B0_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
333
0
35867
TrEMBL
-
Q0K6K2_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
332
0
35935
TrEMBL
-
Q0K3B1_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
356
0
38829
TrEMBL
-
A5N713_CLOK5
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
321
0
35608
TrEMBL
-
D5APA0_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
336
0
36889
TrEMBL
-
G8Q7A2_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
323
0
35143
TrEMBL
-
K4LCV3_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)
307
0
34878
TrEMBL
-
A5N714_CLOK5
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
322
0
36416
TrEMBL
-
F8GM34_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
351
0
38437
TrEMBL
-
A0A2G9H940_9LAMI
303
0
32904
TrEMBL
Chloroplast (Reliability: 3)
K4LXI9_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)
123
0
13738
TrEMBL
-
Q88PG9_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
336
6
36980
TrEMBL
-
D2BLF8_LACLK
Lactococcus lactis subsp. lactis (strain KF147)
338
0
37400
TrEMBL
-
A0A0U5EUH7_9BACT
340
0
38002
TrEMBL
-
Q0KC27_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
319
0
34519
TrEMBL
-
I7GG45_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
332
0
37032
TrEMBL
-
G0EU46_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
343
0
37237
TrEMBL
-
I7GFG0_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
328
5
35060
TrEMBL
-
G0ETM6_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
337
0
35950
TrEMBL
-
A0A2P6PJ04_ROSCH
332
0
36247
TrEMBL
Chloroplast (Reliability: 1)
Q0KBL5_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
343
0
37304
TrEMBL
-
A5N712_CLOK5
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
300
6
32806
TrEMBL
-
D5AL18_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
530
0
58241
TrEMBL
-
A0A8E0L3P8_BURTH
372
0
39815
TrEMBL
-
A5N711_CLOK5
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
312
6
34621
TrEMBL
-
Q3XXB9_ENTFD
Enterococcus faecium (strain ATCC BAA-472 / TX0016 / DO)
317
0
35954
TrEMBL
-
G8Q7A3_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
328
0
35339
TrEMBL
-
G8Q7A5_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
315
6
34734
TrEMBL
-
C9YGK2_CURXX
Curvibacter symbiont subsp. Hydra magnipapillata
277
0
29872
TrEMBL
-
Q88PG8_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
544
0
60974
TrEMBL
-
A5N710_CLOK5
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
539
0
60492
TrEMBL
-
G0EUG9_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
321
0
34106
TrEMBL
-
G8Q7A1_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
504
0
56108
TrEMBL
-
Q88PH0_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
308
6
32963
TrEMBL
-
H7C7K8_BORBU
Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
530
0
60766
TrEMBL
-
Q8PP30_XANAC
Xanthomonas axonopodis pv. citri (strain 306)
294
0
30704
TrEMBL
-
Q8PP31_XANAC
Xanthomonas axonopodis pv. citri (strain 306)
325
0
34730
TrEMBL
-
Q8PP32_XANAC
Xanthomonas axonopodis pv. citri (strain 306)
538
0
59025
TrEMBL
-
Q9WXR2_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
660
0
76186
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32800
x * 32800, deduced from gene sequence, membrane component of permease system
36300
59900
60000
-
x * 60000, recombinant selenium-labeled, detagged soluble AppA, SDS-PAGE
60700
-
x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
60800
-
x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
61000
-
x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
62400
-
x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
36300
x * 36300, deduced from gene sequence, membrane components of permease system
59900
x * 59900, deduced from gene sequence, peptide binding domain of permease
59900
-
x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
oligomer
-
molecular dynamics simulations, with the protein maintaing the overall open structure and shape, and structure modelling
additional information
?
-
x * 60000, recombinant selenium-labeled, detagged soluble AppA, SDS-PAGE
?
-
x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
?
x * 32800, deduced from gene sequence, membrane component of permease system
?
x * 36300, deduced from gene sequence, membrane components of permease system
?
x * 59900, deduced from gene sequence, peptide binding domain of permease
additional information
-
domain organization of AppA and OppA, overview, AppA has a lipid-modified, membrane-anchored extracellular protein binding domain which served as a receptor for the oligopeptide translocation system
additional information
-
the Borrelia burgdorferi oligopeptide permease contains five different substrate binding proteins, i.e. OppA proteins, that interact with the integral membrane components of the transporter, overview
additional information
-
the Borrelia burgdorferi oligopeptide permease contains five different substrate binding proteins, i.e. OppA proteins, that interact with the integral membrane components of the transporter, overview
-
additional information
-
ATP-binding cassette transporter
additional information
-
five proteins OppA, OppB, OppC, OppD and OppF are required for Opp function
additional information
-
five proteins OppA, OppB, OppC, OppD and OppF are required for Opp function
additional information
-
OppB and OppC are responsible for mediating passage of peptides across the cytoplasmic membrane
additional information
-
circular dichroism spectrum of the soluble refolded recombinant OppA and secondary structure of the recombinant protein, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
additional information
-
OppA is complexed with proline-rich endogenous peptides, MALDI tandem mass spectrometry peptide analysis, overview
lipoprotein
-
AppA has a lipid-modified, membrane-anchored extracellular protein binding domain which served as a receptor for the oligopeptide translocation system
lipoprotein
-
the deduced amino acid sequence suggests that all five OppA homologues are lipoproteins
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified soluble form of AppA in complex with a nonapeptide, hanging drop vapour diffusion method, unlabeled enzyme from 12-14% PEG 8000, 0.1-0.2 M zinc acetate, 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, selenium-labeled enzyme from 16-18% PEG 8000, 0.1 M zinc acetate, and 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, cryoprotection by 25% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3-1.6 A resolution, selenium-based anomalous scattering and molecular replacement methods
-
OppA in the open-and closed-liganded conformation, complexed with bradykinin, the nonapeptide RPPGFSPFR, hanging drop vapour diffusion method, 0.001 ml of protein solution are mixed with 10 mg/ml ligand-free OppA, 9 mM Na-MES, pH 6.0, 9 mM NaCl and 1 mM peptide, is mixed with 0.001 ml of reservoir solution containing 0.2 M NaCl, 0.1 M Na-HEPES, pH 7.0, and 20% PEG 6000, 12 weeks at room temperature, X-ray diffraction structure determination and analysis at 1.3 and 2.5 A resolution, respectively
-
sitting drop vapor diffusion method, using 100 mM HEPES pH 7.5, 1.0 M trisodium citrate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D449N
-
OppA mutant, able to grow in presence of 0.02 mg/ml of the toxic tripeptide bialaphos, reduced sporulation rate
E239K
-
OppA mutant, able to grow in presence of 0.32 mg/ml of the toxic tripeptide bialaphos, drastically reduced sporulation rate
E259K
-
OppA mutant, able to grow in presence of 0.16 mg/ml of the toxic tripeptide bialaphos
G299E
-
OppA mutant, able to grow in presence of 0.16 mg/ml of the toxic tripeptide bialaphos, reduced sporulation rate
G337R
-
OppA mutant, able to grow in presence of 0.01 mg/ml of the toxic tripeptide bialaphos, increased sporulation rate
G466E
-
OppA mutant, able to grow in presence of 0.02 mg/ml of the toxic tripeptide bialaphos, reduced sporulation rate
R443H
-
OppA mutant, able to grow in presence of 0.16 mg/ml of the toxic tripeptide bialaphos, drastically reduced sporulation rate
I602C
-
OppA mutant, comparison to the wild-type enzyme in reconstitution in the membrane, substrate binding, and catalysis
V57P/W551P
additional information
V57P/W551P
the mutant essentially shows similar peptide-binding affinity compared to the wild type enzyme
V57P/W551P
-
the mutant essentially shows similar peptide-binding affinity compared to the wild type enzyme
-
additional information
-
identification of mutant strains carrying mini-Tn10 insertions in the oligopeptide permease operon, mutations impair expression of PlcR, a pleiotropic regulator of virulence factors, and cause a deficient haemolytic phenotype. Sporulation of mutants is drastically reduced in LB medium, but normal in sporulation specific medium. In vitro disruption of oppB gene reproduces effect of mini-Tn10 insertions
additional information
construction of cgopt1-silenced mutants by RNAi-mediated silencing, that produce less spores, have reduced pigmentation, and are less pathogenic to plants than the wild-type strain, phenotype, overview
additional information
-
Escherichia coli K12 mutants defective in the expression of OppA exhibit reduced sensitivity to aminoglycosides due to altered permeability of the cell envelope. Strain SS5013, selected for triornithine resistance or with a deletion of the complete opp operon, is defective in uptake of tri- and tetra-peptides but does not show resistance to aminoglycosides
additional information
-
Escherichia coli K12 mutants defective in the expression of OppA exhibit reduced sensitivity to aminoglycosides due to altered permeability of the cell envelope. Strain SS5013, selected for triornithine resistance or with a deletion of the complete opp operon, is defective in uptake of tri- and tetra-peptides but does not show resistance to aminoglycosides
-
additional information
-
OppA and OppBCDF are labeled with fluorescent probes, reconstituted into giant unilamellar vesicles, and the receptor-translocator interactions are investigated by fluorescence correlation spectroscopy, lateral mobility of OppA is reduced in OppBCDF-containing giant unilamellar vesicles distinguishing ligand-bound from ligand-free OppA, overview
additional information
-
mutagenesis of the permease encoded by the Rv1283c-Rv1280c genes in Mtb 1254, Rv1283c-Rv1280c genes are deleted, generation of an Opp loss of function mutant, phenotype. Disruption of the opp locus
additional information
-
OppA, exchange of P-loop motif GKDSSGKS to THASSSAH, no ATP-binding observed, decrease in ATP hydrolysis to 6% of wild-type
additional information
-
isolation of an OPT2 mutant that is sensitive to rapamycin, Zn2+, and bleomycin, in contrast to the wild-type enzyme, overview. An opt2 deletion mutant is defective in vacuole morphology, partial drug resistance is restored by expression of wild-type OPT2, phenotype, overview
additional information
-
opp3 mutant strains show a delayed clotting of milk after casein proteolysis, aur and sspB transcripts are reduced in the opp3 mutant, extracellular protease gene expression analysis of the mutant strain, phenotype, overview
additional information
-
opp3 mutant strains show a delayed clotting of milk after casein proteolysis, aur and sspB transcripts are reduced in the opp3 mutant, extracellular protease gene expression analysis of the mutant strain, phenotype, overview
-
additional information
-
construction of a strain A-20 isogenic oppA null mutant strain showing decreased expression of genes speB, speX, and rofA, and increased transcription of genes speF, sagA, pel, and dppA, expression of genes emm, sda, speJ, speG, rgg, and csrR are unaffected, the oppA mutant causes less mortality and tissue damage compared to the wild-type strain A-20 in mice, expression analysis, overview
additional information
-
construction of diverse mutant strains modified in the ami genes, an increased number of oligopeptide binding proteins increases the bacterial transformation rate, overview
additional information
generation of disruption mutants of the genes oppA1 or oppA2, the mutant show differing oligopeptide binding and translocation specificity, overview
additional information
-
generation of mutant DELTAbldKB-g strain by deleting the entire 1614-bp bldKB-g-coding sequence, phenotype, overview
additional information
-
generation of mutant DELTAbldKB-g strain by deleting the entire 1614-bp bldKB-g-coding sequence, phenotype, overview
-
additional information
-
generation of mutant DELTAbldKB-g strain by deleting the entire 1614-bp bldKB-g-coding sequence, phenotype, overview
additional information
-
generation of mutant DELTAbldKB-g strain by deleting the entire 1614-bp bldKB-g-coding sequence, phenotype, overview
-
additional information
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
additional information
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
additional information
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
additional information
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
additional information
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
additional information
-
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
additional information
Vibrio fluvialis KCTC 2473 / ATCC 33809
-
construction of an oppA knockout mutant by homologous recombination, the mutant strain produced more abundant biofilm than the wild-type strain in brain-heart infusion medium, while both strains do not produce a biofilm at all in minimal medium, the phenotype can be restored by expression of oppA ORF plus promoter, overview
-
additional information
construction of a hly-oppA knockout mutant of Vibrio furnissii, VFYKW1, by the allelic exchange method, the hly-oppA knockout mutant causes less mortality than the wild-type strain when it was inoculated into BALB/c mice, morphology and biofilm production of the hly-oppA knockout mutant, overview
additional information
-
construction of a hly-oppA knockout mutant of Vibrio furnissii, VFYKW1, by the allelic exchange method, the hly-oppA knockout mutant causes less mortality than the wild-type strain when it was inoculated into BALB/c mice, morphology and biofilm production of the hly-oppA knockout mutant, overview
additional information
-
disruption mutants for oppA1, oppA2 and oppB, together with leuB background, leuB oppA2 and leuB oppB mutants only grow on leucine-containing dipeptides, leuB oppA1 mutants also grow on peptide Leu-Leu-Leu. All mutants colonize and survive in nematodes similarly to wild-type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50.6
-
purified recombinant enzyme displays a melting temperature of 50.6°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
OppA without lipid anchor is produced in the cytoplasm of Lactobacillus lactis where endogenous peptides are available for binding. These peptides bind so tightly that they remain associated with the protein throughout the purification, they can be removed from the protein only by guanidium chloride treatment generating ligand-free OppA
-
recombinant His-tagged wild-type and mutant enzymes from Lactococcus lactis by nickel affinity chromatography
-
recombinant refolded and soluble His-tagged OppA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant selenium-labeled maltose-binding fusion protein by amylose affinity chromatography, cleavage of the fusion protein by factor Xa, further purification by ion exchange chromatography and gel filtration, to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and gene organization of the bldK locus, overview
cloning in Escherichia coli JM109, PepT1 translation in Xenopus oocytes
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression using the pAN701 plasmid
expressed in Escherichia coli BL21(DE3) cells
expression of Arabidopsis thaliana AtOPT6 in oocytes by swapping the 5'-untranslated region of AtOPT6 with the 5'-UTR of ScOPT1 from Saccharomyces cerevisiae
-
expression of C-terminal His6-tagged OppA, OppA I602C, and OppBCDF His6-tag on C-terminus of OppC in Lactococcus lactis
-
four opp operons, opp-1, opp-2, opp-3, and opp-4, plus an opp-5A gene encoding a putative peptide-binding protein, DNA and amino acid sequence determination and analysis, opp-1, opp-2, opp-3, and opp-4 operons are polycistronic and opp-5A is monocistronic, transcriptional profiles and sequence comparison. Gene opp-3, which encodes proteins most similar to known peptide transport proteins, displays the highest expression level, overview
-
gene appA, expression of soluble form of AppA fused to maltose-binding protein in Escherichia coli strain B834 periplasm
-
gene oppA, DNA and amino acid sequence determination and analysis, expression of the wild-type enzyme in Escherichia coli strain BL21(DE3)
gene oppA, DNA and amino acid sequence determination and anaylsis, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) as mainly insoluble protein
-
library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis
library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis, expression in Vibrio fluvialis and Escherichia coli
optimization of AtOPT6 expression in oocytes by swapping the 5'-untranslated region of AtOPT6 with the 5'-UTR of ScOPT1 from Saccharomyces cerevisiae
-
the expression of the OppA proteins is individually regulated, alternative sigma factors, RpoS and RpoN, regulate the expression of oppA5 but not that of other oppA genes, while BosR/Fur homologue interacts with the oppA4 promoter and another candidate transcription factor, EbfC, interacts with the oppA5 promoter, overview
-
the two genes oppA1 and oppA2 encoding oligopeptide permeases are located in the clavulinic acid cluster, DNA and amino acid sequence determination and analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CgOpt1 expression is induced by iodoacetic acid. Iodoacetic acid enhances spore formation and causes changes in colony morphology in the wild-type strain, but has no effect on spore formation or colony morphology of the cgopt1-silenced mutants
enzyme expression is upregulated in abscesses and iron-restricted culture medium
transcription of bldKB-g is significantly reduced in the DELTAadpA mutant strain compared with the wild-type strain
enzyme expression is upregulated in abscesses and iron-restricted culture medium
-
enzyme expression is upregulated in abscesses and iron-restricted culture medium
-
-
transcription of bldKB-g is significantly reduced in the DELTAadpA mutant strain compared with the wild-type strain
-
transcription of bldKB-g is significantly reduced in the DELTAadpA mutant strain compared with the wild-type strain
-
transcription of bldKB-g is significantly reduced in the DELTAadpA mutant strain compared with the wild-type strain
-
-
transcription of bldKB-g is significantly reduced in the DELTAadpA mutant strain compared with the wild-type strain
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
OppA and OppBCDF are reconstituted into giant unilamellar vesicles, overview
-
solubilization and refolding of recombinant insoluble His-tagged OppA expressed in Escherichia coli strain BL21(DE3) by dilution with 100fold volumes of refolding buffer, PBS, pH 7.4, containing 1 M urea, 10% glycerol, 0.005% Tween 20, 0.5 mM PMSF and 5 mM DTT, and maintainance under vigorous agitation at 4°C for 8 h
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gallagher, M.P.; Pearce, S.R.; Higgins, C.F.
Identification and localization of the membrane-associated, ATP-binding subunit of the oligopeptide permease of Salmonella typhimurium
Eur. J. Biochem.
180
133-141
1989
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Hiles, I.D.; Gallagher, M.P.; Jamieson, D.J.; Higgins, C.F.
Molecular characterization of the oligopeptide permease of Salmonella typhimurium
J. Mol. Biol.
195
125-142
1987
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Nodwell, J.R.; McGovern, K.; Losick, R.
An oligopeptide permease responsible for the import of an extracellular signal governing aerial mycelium formation in Streptomyces coelicolor
Mol. Microbiol.
22
881-893
1996
Streptomyces coelicolor
brenda
Pearce, S.R.; Mimmack, M.L.; Gallagher, M.P.; Gileadi, U.; Hyde, S.C.; Higgins, C.F.
Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium
Mol. Microbiol.
6
47-57
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Bono, J.L.; Tilly, K.; Stevenson, B.; Hogan, D.; Rosa, P.
Oligopeptide permease in Borrelia burgdorferi: putative peptide-binding components encoded by both chromosomal and plasmid loci
Microbiology
144
1033-1044
1998
Borreliella burgdorferi
brenda
Cosby, W.M.; Vollenbroich, D.; Lee, O.H.; Zuber, P.
Altered srf expression in Bacillus subtilis resulting from changes in culture pH is dependent on the Spo0K oligopeptide permease and the ComQX system of extracellular control
J. Bacteriol.
180
1438-1445
1998
Bacillus subtilis
brenda
Staskawicz, B.J.; Oanopoulos, N.J.
Phaseolotoxin transport in Escherichia coli and Salmonella typhimurium via the oligopeptide permease
J. Bacteriol.
142
474-479
1980
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Andrews, J.C.; Blevins, T.; Short, S.A.
Regulation of peptide transport in Escherichia coli: induction of the trp-linked operon encoding the oligopeptide permease
J. Bacteriol.
165
428-433
1986
Escherichia coli
brenda
Andrews, J.C.; Short, S.A.
opp-lac Operon fusions and transcriptional regulation of the Escherichia coli trp-linked oligopeptide permease
J. Bacteriol.
165
434-442
1986
Escherichia coli
brenda
Orchard, S.S.; Goodrich-Blair, H.
Identification and functional characterization of a Xenorhabdus nematophila oligopeptide permease
Appl. Environ. Microbiol.
70
5621-5627
2004
Xenorhabdus nematophila
brenda
Moutran, A.; Quaggio, R.B.; Balan, A.; Ferreira, L.C.; Ferreira Rde, C.
The oligopeptide permease (Opp) of the plant pathogen Xanthomonas axonopodis pv. citri
Curr. Microbiol.
48
354-359
2004
no activity in Xanthomonas campestris, Xanthomonas axonopodis (Q8PP30), Xanthomonas axonopodis (Q8PP31), Xanthomonas axonopodis (Q8PP32), Xanthomonas axonopodis
brenda
Solomon, J.; Su, L.; Shyn, S.; Grossman, A.D.
Isolation and characterization of mutants of the Bacillus subtilis oligopeptide permease with altered specificity of oligopeptide transport
J. Bacteriol.
185
6425-6433
2003
Bacillus subtilis
brenda
Hopfe, M.; Henrich, B.
OppA, the substrate-binding subunit of the oligopeptide permease, is the major Ecto-ATPase of Mycoplasma hominis
J. Bacteriol.
186
1021-1928
2004
Mycoplasma hominis
brenda
Wang, X.G.; Kidder, J.M.; Scagliotti, J.P.; Klempner, M.S.; Noring, R.; Hu, L.T.
Analysis of differences in the functional properties of the substrate binding proteins of the Borrelia burgdorferi oligopeptide permease (Opp) operon
J. Bacteriol.
186
51-60
2004
Borreliella burgdorferi
brenda
Gominet, M.; Slamti, L.; Gilois, N.; Rose, M.; Lereclus, D.
Oligopeptide permease is required for expression of the Bacillus thuringiensis plcR regulon and for virulence
Mol. Microbiol.
40
963-975
2001
Bacillus thuringiensis
brenda
Lee, E.; Ahn, S.; Park, J.; Lee, J.; Ahn, S.; Kong, I.
Identification of oligopeptide permease (opp) gene cluster in Vibrio fluvialis and characterization of biofilm production by oppA knockout mutation
FEMS Microbiol. Lett.
240
21-30
2004
Vibrio fluvialis (Q5V9R8), Vibrio fluvialis (Q5V9R9), Vibrio fluvialis (Q5V9S0), Vibrio fluvialis (Q5V9S1), Vibrio fluvialis (Q5V9S2), Vibrio fluvialis, Vibrio fluvialis KCTC 2473 / ATCC 33809 (Q5V9R8), Vibrio fluvialis KCTC 2473 / ATCC 33809 (Q5V9R9), Vibrio fluvialis KCTC 2473 / ATCC 33809 (Q5V9S0), Vibrio fluvialis KCTC 2473 / ATCC 33809 (Q5V9S1), Vibrio fluvialis KCTC 2473 / ATCC 33809 (Q5V9S2)
brenda
Wang, C.; Lin, C.; Luo, Y.; Tsai, P.; Lin, Y.; Lin, M.T.; Chuang, W.; Liu, C.; Wu, J.
Effects of oligopeptide permease in group A streptococcal infection
Infect. Immun.
73
2881-2890
2005
Streptococcus sp.
brenda
Lorenzana, L.M.; Perez-Redondo, R.; Santamarta, I.; Martin, J.F.; Liras, P.
Two oligopeptide-permease-encoding genes in the clavulanic acid cluster of Streptomyces clavuligerus are essential for production of the beta-lactamase inhibitor
J. Bacteriol.
186
3431-3438
2004
Streptomyces clavuligerus (Q9LCV8)
brenda
Levdikov, V.M.; Blagova, E.V.; Brannigan, J.A.; Wright, L.; Vagin, A.A.; Wilkinson, A.J.
The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide
J. Mol. Biol.
345
879-892
2004
Bacillus subtilis
brenda
Doeven, M.K.; van den Bogaart, G.; Krasnikov, V.; Poolman, B.
Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy
Biophys. J.
94
3956-3965
2008
Lactococcus lactis
brenda
Hopfe, M.; Henrich, B.
OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells
BMC Microbiol.
8
55
2008
Mycoplasma hominis
brenda
Nakamatsu, E.H.; Fujihira, E.; Ferreira, R.C.; Balan, A.; Costa, S.O.; Ferreira, L.C.
Oligopeptide uptake and aminoglycoside resistance in Escherichia coli K12
FEMS Microbiol. Lett.
269
229-233
2007
Escherichia coli K-12, Escherichia coli K-12 SS320
brenda
Balan, A.; Ferreira, R.C.; Ferreira, L.C.
Production of the refolded oligopeptide-binding protein (OppA) encoded by the citrus pathogen Xanthomonas axonopodis pv. Citri
Genet. Mol. Res.
7
117-126
2008
Xanthomonas axonopodis
brenda
Medrano, M.S.; Ding, Y.; Wang, X.G.; Lu, P.; Coburn, J.; Hu, L.T.
Regulators of expression of the oligopeptide permease A proteins of Borrelia burgdorferi
J. Bacteriol.
189
2653-2659
2007
Borreliella burgdorferi, Borreliella burgdorferi N40
brenda
Hiron, A.; Borezee-Durant, E.; Piard, J.C.; Juillard, V.
Only one of four oligopeptide transport systems mediates nitrogen nutrition in Staphylococcus aureus
J. Bacteriol.
189
5119-5129
2007
Staphylococcus aureus
brenda
Wu, T.K.; Wang, Y.K.; Chen, Y.C.; Feng, J.M.; Liu, Y.H.; Wang, T.Y.
Identification of a Vibrio furnissii oligopeptide permease and characterization of its in vitro hemolytic activity
J. Bacteriol.
189
8215-8223
2007
Vibrio furnissii (Q0PRU9), Vibrio furnissii
brenda
Borezee-Durant, E.; Hiron, A.; Piard, J.C.; Juillard, V.
Dual role of the oligopeptide permease Opp3 during growth of Staphylococcus aureus in milk
Appl. Environ. Microbiol.
75
3355-3357
2009
Staphylococcus aureus, Staphylococcus aureus RN6390
brenda
Amberg, J.J.; Myr, C.; Kamisaka, Y.; Jordal, A.E.; Rust, M.B.; Hardy, R.W.; Koedijk, R.; Ronnestad, I.
Expression of the oligopeptide transporter, PepT1, in larval Atlantic cod (Gadus morhua)
Comp. Biochem. Physiol. B
150
177-182
2008
Gadus morhua (A8YV68), Gadus morhua
brenda
Berntsson, R.P.; Doeven, M.K.; Fusetti, F.; Duurkens, R.H.; Sengupta, D.; Marrink, S.J.; Thunnissen, A.M.; Poolman, B.; Slotboom, D.J.
The structural basis for peptide selection by the transport receptor OppA
EMBO J.
28
1332-1340
2009
Lactococcus lactis
brenda
Gardan, R.; Besset, C.; Guillot, A.; Gitton, C.; Monnet, V.
The oligopeptide transport system is essential for the development of natural competence in Streptococcus thermophilus strain LMD-9
J. Bacteriol.
191
4647-4655
2009
Streptococcus thermophilus
brenda
Aouida, M.; Khodami-Pour, A.; Ramotar, D.
Novel role for the Saccharomyces cerevisiae oligopeptide transporter Opt2 in drug detoxification
Biochem. Cell Biol.
87
653-661
2009
Saccharomyces cerevisiae
brenda
Chague, V.; Maor, R.; Sharon, A.
CgOpt1, a putative oligopeptide transporter from Colletotrichum gloeosporioides that is involved in responses to auxin and pathogenicity
BMC Microbiol.
9
173
2009
Colletotrichum aeschynomenes (C6ZRH8)
brenda
Flores-Valdez, M.A.; Morris, R.P.; Laval, F.; Daffe, M.; Schoolnik, G.K.
Mycobacterium tuberculosis modulates its cell surface via an oligopeptide permease (Opp) transport system
FASEB J.
23
4091-4104
2009
Mycobacterium tuberculosis
brenda
Sangaletti, R.; Terova, G.; Peres, A.; Bossi, E.; Cora, S.; Saroglia, M.
Functional expression of the oligopeptide transporter PepT1 from the sea bass (Dicentrarchus labrax)
Pflugers Arch.
459
47-54
2009
Dicentrarchus labrax
brenda
Pike, S.; Patel, A.; Stacey, G.; Gassmann, W.
Arabidopsis OPT6 is an oligopeptide transporter with exceptionally broad substrate specificity
Plant Cell Physiol.
50
1923-1932
2009
Arabidopsis thaliana, Saccharomyces cerevisiae
brenda
Akanuma, G.; Ueki, M.; Ishizuka, M.; Ohnishi, Y.; Horinouchi, S.
Control of aerial mycelium formation by the BldK oligopeptide ABC transporter in Streptomyces griseus
FEMS Microbiol. Lett.
315
54-62
2011
Streptomyces coelicolor, Streptomyces griseus, Streptomyces coelicolor A3(2), Streptomyces griseus IFO 13350
brenda
Jones, M.M.; Johnson, A.; Koszelak-Rosenblum, M.; Kirkham, C.; Brauer, A.L.; Malkowski, M.G.; Murphy, T.F.
Role of the oligopeptide permease ABC transporter of Moraxella catarrhalis in nutrient acquisition and persistence in the respiratory tract
Infect. Immun.
82
4758-4766
2014
Moraxella catarrhalis, Moraxella catarrhalis 035E
brenda
Ding, Y.; Fu, Y.; Lee, J.C.; Hooper, D.C.
Staphylococcus aureus NorD, a putative efflux pump coregulated with the Opp1 oligopeptide permease, contributes selectively to fitness in vivo
J. Bacteriol.
194
6586-6593
2012
Staphylococcus aureus, Staphylococcus aureus MW2
brenda
Wang, G.; Li, D.; Ma, X.; An, H.; Zhai, Z.; Ren, F.; Hao, Y.
Functional role of oppA encoding an oligopeptide-binding protein from Lactobacillus salivarius Ren in bile tolerance
J. Ind. Microbiol. Biotechnol.
42
1167-1174
2015
Ligilactobacillus salivarius
brenda
Danelishvili, L.; Stang, B.; Bermudez, L.E.
Identification of Mycobacterium avium genes expressed during invivo infection and the role of the oligopeptide transporter OppA in virulence
Microb. Pathog.
76
67-76
2014
Mycobacterium avium
brenda
Choudhury, H.G.; Tong, Z.; Mathavan, I.; Li, Y.; Iwata, S.; Zirah, S.; Rebuffat, S.; van Veen, H.W.; Beis, K.
Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state
Proc. Natl. Acad. Sci. USA
111
9145-9150
2014
Escherichia coli
brenda
Yoon, H.J.; Kim, H.J.; Mikami, B.; Yu, Y.G.; Lee, H.H.
Crystal structure of a putative oligopeptide-binding periplasmic protein from a hyperthermophile
Extremophiles
20
723-731
2016
Thermotoga maritima (Q9WXR2), Thermotoga maritima ATCC 43589 (Q9WXR2)
brenda
Groshong, A.M.; Dey, A.; Bezsonova, I.; Caimano, M.J.; Radolf, J.D.
Peptide uptake is essential for Borrelia burgdorferi viability and involves structural and regulatory complexity of its oligopeptide transporter
mBio
8
e02047-17
2017
Borreliella burgdorferi (H7C7K8), Borreliella burgdorferi B31 (H7C7K8)
brenda
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EXTERNAL LINKS (specific for EC-Number 7.4.2.6)
Transporter Classification Database (TCDB): 3.A.1.209.2
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Release 2023.1 (January 2023)
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