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HELPY:HCPB
Contents
Species (Taxon ID) | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacterpylori). (85962) | |
Gene Name(s) | hcpB | |
Protein Name(s) | Beta-lactamase HcpB
Cysteine-rich protein B | |
External Links | ||
UniProt | O25103 | |
EMBL | AE000511 | |
PIR | H64561 | |
PDB | 1KLX | |
PDBsum | 1KLX | |
ProteinModelPortal | O25103 | |
SMR | O25103 | |
DIP | DIP-3342N | |
IntAct | O25103 | |
MINT | MINT-160080 | |
STRING | 85962.HP0336 | |
PRIDE | O25103 | |
EnsemblBacteria | AAD07408 | |
PATRIC | 20591907 | |
eggNOG | COG0790 | |
OMA | SIACEAN | |
OrthoDB | EOG6TJ7WZ | |
BioCyc | HPY:HP0336-MONOMER | |
EvolutionaryTrace | O25103 | |
Proteomes | UP000000429 | |
GO | GO:0008800 GO:0008152 GO:0046677 | |
Gene3D | 1.25.40.10 | |
InterPro | IPR006597 IPR011990 | |
Pfam | PF08238 | |
SMART | SM00671 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0008800 |
beta-lactamase activity |
ECO:0000314 |
F |
Table 1: Purified HcpB hydrolyzes several antibiotics by opening of the beta-lactam ring, which was monitored by absorption variation. |
complete | |||||
enables |
GO:0008800 |
beta-lactamase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008800 |
beta-lactamase activity |
ECO:0000501 |
evidence 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:0046677 |
response to antibiotic |
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 Luthy, L et al. (2002) The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein. J. Biol. Chem. 277 10187-93 PubMed GONUTS page