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Literature summary for 2.4.1.129 extracted from

  • Tsui, H.C.; Zheng, J.J.; Magallon, A.N.; Ryan, J.D.; Yunck, R.; Rued, B.E.; Bernhardt, T.G.; Winkler, M.E.
    Suppression of a deletion mutation in the gene encoding essential PBP2b reveals a new lytic transglycosylase involved in peripheral peptidoglycan synthesis in Streptococcus pneumoniae D39 (2016), Mol. Microbiol., 100, 1039-1065 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene pbp2A, recombinant expression of FLAG-tagged wild-type and mutant enzymes in Streptococcus pneumoniae strain D39 DELTAcps/DELTAmltG obtained from strain IU7260 Streptococcus pneumoniae
gene penA or pbp2B, genotyping, recombinant expression in Streptococcus pneumoniae strain IU1824, i.e. D39 DELTAcps Streptococcus pneumoniae

Protein Variants

Protein Variants Comment Organism
G494E naturally occuring mutation, the mutant cannot be transformed with a DELTApbp2a deletion and shows the small-cell phenotype characteristic of DELTApbp1a mutants, reduced activity compared to wild-type Streptococcus pneumoniae
additional information construction of DELTA pbp2A deletion mutants. Domain architecture of PBP1a, TP active site motifs and mapped mutations in gene pbp1a in DELTAmltG suppressor strains. DELTApbp2A/DELTAmltG mutant phenotype, overview Streptococcus pneumoniae
additional information construction of DELTA pbp2B deletion mutants. Mutations in spd_1346 (mltG) suppress a DELTApbp2b deletion mutation. DELTApbp2B/DELTAmltG mutant phenotype, overview Streptococcus pneumoniae
S89F naturally occuring mutation, reduced activity compared to wild-type. The mutant can be transformed with a DELTApbp2a deletion. pbp1a(S89F) mutants shows an intermediate size Streptococcus pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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Streptococcus pneumoniae 16020
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membrane transmembrane protein Streptococcus pneumoniae 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol Streptococcus pneumoniae
-
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol Streptococcus pneumoniae ATCC BAA-334
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[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae A0A0H2URT5
-
-
Streptococcus pneumoniae P0A3M5
-
-
Streptococcus pneumoniae ATCC BAA-334 A0A0H2URT5
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-
Streptococcus pneumoniae ATCC BAA-334 P0A3M5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Streptococcus pneumoniae [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Streptococcus pneumoniae ATCC BAA-334 [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
?

Subunits

Subunits Comment Organism
More domain architecture of PBP1a Streptococcus pneumoniae

Synonyms

Synonyms Comment Organism
class A penicillin-binding protein
-
Streptococcus pneumoniae
class B penicillin-binding protein
-
Streptococcus pneumoniae
PBP2A
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Streptococcus pneumoniae
PBP2b
-
Streptococcus pneumoniae
PenA
-
Streptococcus pneumoniae

General Information

General Information Comment Organism
evolution Streptococcus pneumoniae contains three class A (PBP1a, PBP2a and PBP1b) and two class B (PBP2x and PBP2b) enzymes. PBP1a and PBP2a are not equivalent Streptococcus pneumoniae
malfunction DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a. The reduction of cell width and size of DELTApbp1a mutants compared to those of wild-type parent cells. Mutations in pbp1a suppress the DELTAmltG mutations Streptococcus pneumoniae
malfunction mutations that inactivate the pneumococcal YceG-domain protein, Spd_1346 (renamed MltG), remove the requirement for PBP2b. DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a, which possesses TP and transglycosylase (TG) activities Streptococcus pneumoniae
metabolism the pneumococcal YceG-domain protein MltG releases anchored peptidoglycan (PG) glycan strands synthesized by PBP1a for crosslinking by a PBP2b:RodA complex in peripheral PG synthesis Streptococcus pneumoniae
additional information domain architecture of PBP1a Streptococcus pneumoniae
additional information the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA Streptococcus pneumoniae
physiological function peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. Class A PBP1a, which possesses TP and transglycosylase (TG) activities Streptococcus pneumoniae
physiological function peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. In the pathogen Streptococcus pneumoniae (pneumococcus), side-wall (peripheral) peptidoglycan (PG) synthesis emanates from midcells and is catalyzed by the essential class B penicillin-binding protein PBP2b transpeptidase (TP). Class B PBP2x and PBP2b are essential for growth and required for septal and peripheral PG synthesis, respectively, in dividing Streptococcus pneumoniae cells. Pbp2b is essential in unencapsulated or encapsulated wild-type D39 strains Streptococcus pneumoniae