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ECOLI:AMPH
Contents
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 |
ECO:0000316 |
UniProtKB:p02918 UniProtKB:p0aeb2
|
P |
fig 9 |
complete | ||||
involved_in |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0008360 |
regulation of cell shape |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004180 |
carboxypeptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004175 |
endopeptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008658 |
penicillin binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0997 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0008360 |
regulation of cell shape |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004180 |
carboxypeptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0071555 |
cell wall organization |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ 2.0 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
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