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Information on EC 7.4.2.12 - ABC-type cystine transporter
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EC Tree
7.4.2.12 ABC-type cystine transporterIUBMB Comments
ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity import of trace cystine. The enzyme from Escherichia coli K-12 can import both isomers of cystine and a variety of related molecules including djenkolate, lanthionine, diaminopimelate and homocystine.
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Word Map
- 7.4.2.12
- sulfur
- l-cysteine
-
regulon
- mutans
- s-methyl-l-cysteine
-
l-djenkolic
- l-selenocystine
-
ligand-free
-
l-aspartic
- cysb
-
futile
- deinococcus
-
lysr-type
- geothermalis
-
symporter
-
fenton
- maleate
- l-serine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
+
+
+
+
L-cystine-[cystine-binding protein][side 1]
=
+
+
+
[cystine-binding protein][side 1]
+
+
=
+
+
+
+
+
D-cystine-[cystine-binding protein][side 1]
=
+
+
+
[cystine-binding protein][side 1]
Synonyms
tcyabc, l-cystine transporter, cystine importer, fliy-yecsc, l-cystine abc transporter, ytmjklmn, cystine abc transporter, yckkji, tcyabc transporter, tcyjln, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cystine ABC importer
cystine ABC transporter
cystine specific transport system
cystine transporting ATPase
-
-
-
-
cystine-specific ABC transporter
L-cystine ABC transporter
TcyA
tcyABC
TcyABC transporter
TcyB
TcyC
tcyJKLMN
YckKJI
ytmI
YtmJKLMN
cystine ABC transporter
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + D-cystine-[cystine-binding protein][side 1] = ADP + phosphate + D-cystine[side 2] + [cystine-binding protein][side 1]
(2)
-
-
-
ATP + H2O + L-cystine-[cystine-binding protein][side 1] = ADP + phosphate + L-cystine[side 2] + [cystine-binding protein][side 1]
(1)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, cystine-importing)
ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity import of trace cystine. The enzyme from Escherichia coli K-12 can import both isomers of cystine and a variety of related molecules including djenkolate, lanthionine, diaminopimelate and homocystine.
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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 + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
ATP + H2O + diaminopimelate-[diaminopimelate-binding protein](side 1)
ADP + phosphate + diaminopimelate(side 2) + [diaminopimelate-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein II][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein II][side 1]
ATP + H2O + L-cystine-[cystine-binding protein I][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein I][side 1]
ATP + H2O + L-cystine-[cystine-binding protein Ngo0372](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein Ngo0372](side 1)
ATP + H2O + L-cystine-[cystine-binding protein TcyA](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein TcyA](side 1)
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
ATP + H2O + L-cystine-[cystine-binding protein][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + selenocystine-[cystine-binding protein Ngo0372](side 1)
ADP + phosphate + selenocystine(side 2) + [cystine-binding protein Ngo0372](side 1)
ATP + H2O + selenocystine-[cystine-binding protein](side 1)
ADP + phosphate + selenocystine(side 2) + [cystine-binding protein](side 1)
ATP + H2O + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein II][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein II][side 1]
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein II][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein II][side 1]
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein I][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein I][side 1]
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein I][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein I][side 1]
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein Ngo0372](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein Ngo0372](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein Ngo0372](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein Ngo0372](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein TcyA](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein TcyA](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein TcyA](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein TcyA](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + selenocystine-[cystine-binding protein Ngo0372](side 1)
ADP + phosphate + selenocystine(side 2) + [cystine-binding protein Ngo0372](side 1)
-
-
-
-
?
ATP + H2O + selenocystine-[cystine-binding protein Ngo0372](side 1)
ADP + phosphate + selenocystine(side 2) + [cystine-binding protein Ngo0372](side 1)
-
-
-
-
?
ATP + H2O + selenocystine-[cystine-binding protein](side 1)
ADP + phosphate + selenocystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + selenocystine-[cystine-binding protein](side 1)
ADP + phosphate + selenocystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
additional information
?
-
-
methyl-L-cysteine and L-cysteine are no substrates
-
-
?
additional information
?
-
-
methyl-L-cysteine and L-cysteine are no substrates
-
-
?
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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 + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
ATP + H2O + L-cystine-[cystine-binding protein TcyA](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein TcyA](side 1)
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
ATP + H2O + L-cystine-[cystine-binding protein][side 1]
ADP + phosphate + L-cystine[side 2] + [cystine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + D-cystine-[cystine-binding protein](side 1)
ADP + phosphate + D-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein TcyA](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein TcyA](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein TcyA](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein TcyA](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
ATP + H2O + L-cystine-[cystine-binding protein](side 1)
ADP + phosphate + L-cystine(side 2) + [cystine-binding protein](side 1)
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
oxidized glutathione
-
enzyme YtmJKLMN shows less than 10% inhibition at 0.05 mM
additional information
-
not inhibited by FeSO4, L-arginine, L-glutamine, L-glutamate, L-leucine, and L-methionine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
YtlI
-
the YtlI regulator activates the transcription of the ytmI operon encoding an L-cystine ABC transporter, a riboflavin kinase, and proteins of unknown function
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The Staphylococcus aureus Cystine Transporters TcyABC and TcyP Facilitate Nutrient Sulfur Acquisition during Infection.
Starvation
TcyR regulates l-cystine uptake via the TcyABC transporter in Streptococcus mutans.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000496
L-cystine-[cystine-binding protein][side 1]
-
at pH 6.5 and 37°C
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
enzyme form FliY-YecSC is essential for import of trace cystine, whereas enzyme form YdjN is the predominant importer when cystine is more abundant. YdjN is responsible for the rapid cystine import and H2O2 sensitivity of Escherichia coli that has been pre-grown in sulfate medium, but the rapid transport and H2O2 sensitivity are absent if cells have been pre-grown in cystine medium
metabolism
-
the enzyme imports L-cystine from the periplasm to the cytoplasm
physiological function
-
the enzyme contributes to hydrogen peroxide tolerance. The L-cystine/L-cystine shuttle system plays a role of detoxification of hydrogen peroxide before lipid peroxidation occurs, and then specifically prevents damage to membrane lipids
physiological function
-
the enzyme is required for growth of Streptococcus mutans on glutathione as the sole source of sulfur
physiological function
-
the enzyme is required for growth of Streptococcus mutans on glutathione as the sole source of sulfur
-
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complex with L-cystine, L-cysteine, L-arginine and citrate, sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate buffer, pH 5.6 containing 2.0 M ammonium sulfate
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Select nickel affinity column chromatography and Superdex S200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased with L-methionine
enzyme expression is reduced with sulfate
enzyme expression is upregulated under cystine starvation and by the transcriptional activator CysR
the enzyme is strongly induced by the regulon CysB response to sulfur scarcity
-
the transcriptional regulator TcyR negatively regulates the expression of the enzyme
enzyme expression is upregulated under cystine starvation and by the transcriptional activator CysR
-
enzyme expression is upregulated under cystine starvation and by the transcriptional activator CysR
-
-
the transcriptional regulator TcyR negatively regulates the expression of the enzyme
-
the transcriptional regulator TcyR negatively regulates the expression of the enzyme
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumar, P.; Kesari, P.; Kokane, S.; Ghosh, D.K.; Kumar, P.; Sharma, A.K.
Crystal structures of a putative periplasmic cystine-binding protein from Candidatus Liberibacter asiaticus insights into an adapted mechanism of ligand binding
FEBS J.
286
3450-3472
2019
Candidatus Liberibacter asiaticus (C6XGT2), Candidatus Liberibacter asiaticus, Candidatus Liberibacter asiaticus psy62 (C6XGT2)
brenda
Kim, J.; Senadheera, D.; Levesque, C.; Cvitkovitch, D.
TcyR regulates L-cystine uptake via the TcyABC transporter in Streptococcus mutans
FEMS Microbiol. Lett.
328
114-121
2012
Streptococcus mutans, Streptococcus mutans UA159
brenda
Burguiere, P.; Auger, S.; Hullo, M.; Danchin, A.; Martin-Verstraete, I.
Three different systems participate in L-cystine uptake in Bacillus subtilis
J. Bacteriol.
186
4875-4884
2004
Bacillus subtilis, Bacillus subtilis 168
brenda
Burguiere, P.; Fert, J.; Guillouard, I.; Auger, S.; Danchin, A.; Martin-Verstraete, I.
Regulation of the Bacillus subtilis ytmI operon, involved in sulfur metabolism
J. Bacteriol.
187
6019-6030
2005
Bacillus subtilis, Bacillus subtilis 168
brenda
Chonoles Imlay, K.R.; Korshunov, S.; Imlay, J.A.
Physiological roles and adverse effects of the two cystine importers of Escherichia coli
J. Bacteriol.
197
3629-3644
2015
Escherichia coli
brenda
Berger, E.; Heppel, L.
A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli
J. Biol. Chem.
247
7684-7694
1972
Escherichia coli, Escherichia coli ATCC 9637
brenda
Bulut, H.; Moniot, S.; Licht, A.; Scheffel, F.; Gathmann, S.; Saenger, W.; Schneider, E.
Crystal structures of two solute receptors for L-cystine and L-cysteine, respectively, of the human pathogen Neisseria gonorrhoeae
J. Mol. Biol.
415
560-572
2012
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
brenda
Vergauwen, B.; Verstraete, K.; Senadheera, D.B.; Dansercoer, A.; Cvitkovitch, D.G.; Guedon, E.; Savvides, S.N.
Molecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans
Mol. Microbiol.
89
288-303
2013
Streptococcus mutans, Streptococcus mutans UA159
brenda
Ohtsu, I.; Kawano, Y.; Suzuki, M.; Morigasaki, S.; Saiki, K.; Yamazaki, S.; Nonaka, G.; Takagi, H.
Uptake of L-cystine via an ABC transporter contributes defense of oxidative stress in the L-cystine export-dependent manner in Escherichia coli
PLoS ONE
10
e0120619
2015
Escherichia coli
brenda
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EXTERNAL LINKS (specific for EC-Number 7.4.2.12)
Transporter Classification Database (TCDB): 3.A.1.3.10
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Release 2023.1 (January 2023)
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