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HELM1:D3UHB3
Contents
| Species (Taxon ID) | Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 /12198) (Campylobacter mustelae). (679897) | |
| Gene Name(s) | cheV2 (ECO:0000313 with EMBL:CBG39885.1) | |
| Protein Name(s) | Putative chemotaxis protein CheV2 similar to H. pylori CheV2/HP0616 (ECO:0000313 with EMBL:CBG39885.1) | |
| External Links | ||
| UniProt | D3UHB3 | |
| EMBL | FN555004 | |
| RefSeq | WP_013022968.1 YP_003516623.1 | |
| EnsemblBacteria | CBG39885 | |
| GeneID | 8865850 | |
| KEGG | hms:HMU06240 | |
| PATRIC | 35378682 | |
| HOGENOM | HOG000062244 | |
| KO | K03415 | |
| OMA | IINSSMS | |
| BioCyc | HMUS679897:GJBK-650-MONOMER | |
| Proteomes | UP000001522 | |
| GO | GO:0005622 GO:0004871 GO:0006935 GO:0000160 | |
| InterPro | IPR024181 IPR002545 IPR011006 IPR001789 | |
| Pfam | PF01584 PF00072 | |
| PIRSF | PIRSF002867 | |
| SMART | SM00260 SM00448 | |
| SUPFAM | SSF50341 SSF52172 | |
| PROSITE | PS50851 PS50110 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0006811 |
ion transport |
ECO:0000315 |
P |
Figure 1, 2, and 3A all support the idea that Q58C is a mutant. This is because it creates dimers as the paper suggested it would. |
complete | |||||
|
involved_in |
GO:0000160 |
phosphorelay signal transduction system |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0007165 |
signal transduction |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Karasawa, A et al. (2010) Intermolecular cross-linking of monomers in Helicobacter pylori Na+/H+ antiporter NhaA at the dimer interface inhibits antiporter activity. Biochem. J. 426 99-108 PubMed GONUTS page