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ECOLI:AMPH

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ampH (synonyms: yaiH)
Protein Name(s) D-alanyl-D-alanine-carboxypeptidase/endopeptidase AmpH

DD-alanine-endopeptidase DD-carboxypeptidase Penicillin-binding protein AmpH

External Links
UniProt P0AD70
EMBL U73857
U00096
AP009048
X54153
PIR H64765
RefSeq NP_414910.1
YP_488669.1
ProteinModelPortal P0AD70
SMR P0AD70
DIP DIP-47910N
IntAct P0AD70
STRING 511145.b0376
MEROPS S12.012
PaxDb P0AD70
PRIDE P0AD70
EnsemblBacteria AAC73479
BAE76157
GeneID 12930488
946904
KEGG ecj:Y75_p0365
eco:b0376
PATRIC 32115891
EchoBASE EB2708
EcoGene EG12867
eggNOG COG1680
HOGENOM HOG000117477
InParanoid P0AD70
OMA TTKYFLA
OrthoDB EOG6CZQN4
PhylomeDB P0AD70
BioCyc EcoCyc:EG12867-MONOMER
ECOL316407:JW5052-MONOMER
MetaCyc:EG12867-MONOMER
PRO PR:P0AD70
Proteomes UP000000318
UP000000625
Genevestigator P0AD70
GO GO:0005886
GO:0004180
GO:0004175
GO:0008658
GO:0071555
GO:0009253
GO:0008360
Gene3D 3.40.710.10
InterPro IPR001466
IPR012338
Pfam PF00144
SUPFAM SSF56601

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0000902

cell morphogenesis

PMID:9324260[1]

ECO:0000316

UniProtKB:p02918 UniProtKB:p0aeb2


P

fig 9

complete
CACAO 3602

involved_in

GO:0009253

peptidoglycan catabolic process

PMID:22001512[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:9324260[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

PMID:22001512[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:22001512[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

PMID:9324260[1]

ECO:0000314

direct assay evidence used in manual assertion

F

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

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

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

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

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

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: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

Notes

References

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

  1. 1.0 1.1 1.2 Henderson, TA et al. (1997) AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179 6112-21 PubMed GONUTS page
  2. 2.0 2.1 2.2 González-Leiza, SM et al. (2011) AmpH, a bifunctional DD-endopeptidase and DD-carboxypeptidase of Escherichia coli. J. Bacteriol. 193 6887-94 PubMed GONUTS page