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ECOLI:PBP2

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) mrdA (synonyms: pbpA)
Protein Name(s) Penicillin-binding protein 2

PBP-2

External Links
UniProt P0AD65
EMBL X04516
U82598
U00096
AP009048
M22857
PIR C24995
RefSeq NP_415168.1
YP_488926.1
ProteinModelPortal P0AD65
SMR P0AD65
DIP DIP-48190N
IntAct P0AD65
STRING 511145.b0635
ChEMBL CHEMBL2354204
DrugBank DB01327
DB01413
DB01328
DB01329
DB00438
DB01415
DB00303
DB01598
DB00948
PaxDb P0AD65
PRIDE P0AD65
EnsemblBacteria AAC73736
BAA35282
GeneID 12930918
945240
KEGG ecj:Y75_p0625
eco:b0635
PATRIC 32116453
EchoBASE EB0601
EcoGene EG10606
eggNOG COG0768
HOGENOM HOG000266120
InParanoid P0AD65
KO K05515
OMA ARNYSAY
OrthoDB EOG6N0HHV
PhylomeDB P0AD65
BioCyc EcoCyc:EG10606-MONOMER
ECOL316407:JW0630-MONOMER
MetaCyc:EG10606-MONOMER
UniPathway UPA00219
PRO PR:P0AD65
Proteomes UP000000318
UP000000625
Genevestigator P0AD65
GO GO:0005887
GO:0008144
GO:0008658
GO:0071972
GO:0009002
GO:0071555
GO:0009252
GO:0006508
GO:0008360
GO:0046677
GO:0042493
Gene3D 3.40.710.10
InterPro IPR012338
IPR005311
IPR001460
IPR017790
Pfam PF03717
PF00905
SUPFAM SSF56519
SSF56601
TIGRFAMs TIGR03423

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009252

peptidoglycan biosynthetic process

PMID:PMC2681889

ECO:0000315

P

figure 7 shows penicilin binding protein 2 untethers the incorporation of peptidoglycan in the cell walls

complete
CACAO 5129

enables

GO:0071972

peptidoglycan L,D-transpeptidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10606
PANTHER:PTN000771407

F

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10606
PANTHER:PTN000771406

P

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10341
EcoGene:EG10606
PANTHER:PTN000771406

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10341
EcoGene:EG10606
PANTHER:PTN000771406

C

Seeded From UniProt

complete

enables

GO:0071972

peptidoglycan L,D-transpeptidase activity

PMID:6297485[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0046677

response to antibiotic

PMID:1103132[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

PMID:1103132[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:1103132[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:1103132[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

PMID:3326629[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

PMID:18390656[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

PMID:11418550[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:18390656[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:18250190[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:17470659[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

PMID:8760906[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

PMID:18390656[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:1731901[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:3009484[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:3894330[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:18390656[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:17513478[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:12519203[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:11418550[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008144

drug binding

PMID:18250190[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008144

drug binding

PMID:17470659[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008144

drug binding

PMID:12886052[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008144

drug binding

PMID:12709336[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001460
InterPro:IPR005311
InterPro:IPR017790
InterPro:IPR036138

F

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017790

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017790

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017790

C

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.16.4

F

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432224

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432224

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432224

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0573
UniPathway:UPA00219

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0121

F

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0133

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. Ishino, F et al. (1982) A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli. Biochem. Biophys. Res. Commun. 109 689-96 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Spratt, BG (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. 72 2999-3003 PubMed GONUTS page
  4. Buchnik, D et al. () Effects of temperature inactivation of penicillin-binding protein 2 on envelope growth in Escherichia coli. Ann. Inst. Pasteur Microbiol. 138 537-47 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 Uehara, T & Park, JT (2008) Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation. J. Bacteriol. 190 3914-22 PubMed GONUTS page
  6. 6.0 6.1 de Pedro, MA et al. (2001) Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2. J. Bacteriol. 183 4115-26 PubMed GONUTS page
  7. 7.0 7.1 Davies, TA et al. (2008) Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 52 1510-2 PubMed GONUTS page
  8. 8.0 8.1 Davies, TA et al. (2007) Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae. Antimicrob. Agents Chemother. 51 2621-4 PubMed GONUTS page
  9. Signoretto, C et al. (1996) Modified peptidoglycan chemical composition in shape-altered Escherichia coli. Microbiology (Reading, Engl.) 142 ( Pt 8) 1919-26 PubMed GONUTS page
  10. Adachi, H et al. (1992) Active-site residues of the transpeptidase domain of penicillin-binding protein 2 from Escherichia coli: similarity in catalytic mechanism to class A beta-lactamases. Biochemistry 31 430-7 PubMed GONUTS page
  11. Ishino, F et al. (1986) Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein. J. Biol. Chem. 261 7024-31 PubMed GONUTS page
  12. Begg, KJ & Donachie, WD (1985) Cell shape and division in Escherichia coli: experiments with shape and division mutants. J. Bacteriol. 163 615-22 PubMed GONUTS page
  13. Legaree, BA et al. (2007) Overproduction of penicillin-binding protein 2 and its inactive variants causes morphological changes and lysis in Escherichia coli. J. Bacteriol. 189 4975-83 PubMed GONUTS page
  14. Den Blaauwen, T et al. (2003) Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol. Microbiol. 47 539-47 PubMed GONUTS page
  15. Dalhoff, A et al. (2003) Target affinities of faropenem to and its impact on the morphology of gram-positive and gram-negative bacteria. Chemotherapy 49 172-83 PubMed GONUTS page
  16. Jamieson, CE et al. (2003) In vitro and in vivo activities of AM-112, a novel oxapenem. Antimicrob. Agents Chemother. 47 1652-7 PubMed GONUTS page