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BACSU:MCSA
Contents
| Species (Taxon ID) | Bacillus subtilis (strain 168). (224308) | |
| Gene Name(s) | mcsA (synonyms: yacH) | |
| Protein Name(s) | Protein-arginine kinase activator protein | |
| External Links | ||
| UniProt | P37569 | |
| EMBL | D26185 AL009126 | |
| PIR | S66113 | |
| RefSeq | NP_387965.1 WP_009966297.1 | |
| ProteinModelPortal | P37569 | |
| SMR | P37569 | |
| STRING | 224308.Bsubs1_010100000435 | |
| PaxDb | P37569 | |
| EnsemblBacteria | CAB11860 | |
| GeneID | 936845 | |
| KEGG | bsu:BSU00840 | |
| PATRIC | 18971673 | |
| eggNOG | ENOG4108Z0C COG3880 | |
| HOGENOM | HOG000218089 | |
| InParanoid | P37569 | |
| KO | K19411 | |
| OMA | HYTQIIN | |
| OrthoDB | EOG6XDH1X | |
| PhylomeDB | P37569 | |
| BioCyc | BSUB:BSU00840-MONOMER | |
| Proteomes | UP000001570 | |
| Gene3D | 4.10.860.10 | |
| InterPro | IPR001943 IPR025542 | |
| Pfam | PF02151 | |
| PIRSF | PIRSF015034 | |
| SUPFAM | SSF46600 | |
| PROSITE | PS50151 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0006508 |
proteolysis |
ECO:0000315 |
P |
McsA play a role in regulating transcription of CtsR-dependent heat shock genes. Figure 5- In the mcsA mutants, CtsR-dependent heat shock proteins under non-stressed conditions were increased when compared with the wild-type. Figure 6B- In nonstressed McsA mutant cells, the CtsR level was lower than it was in the wild type. After heat shock, CtsR levels in the mutant decreased suggestin that CtsR is less stable without McsA. The half-life of CtsR was also lower in cells lacking McsA |
complete | |||||
| GO:0006508 |
proteolysis |
ECO:0000314 |
P |
Through gel mobility shift experiments (Figure 6), it was shown that addition of McsA does not influence he CtsR DNA binding activity while excess (12-fold) McsA could promote CtsR-dependent DNA binding. |
complete | |||||
|
involved_in |
GO:1990170 |
stress response to cadmium ion |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002212748 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:1990169 |
stress response to copper ion |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002212748 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0050897 |
cobalt ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002212748 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0046870 |
cadmium ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002212748 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002212748 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0005507 |
copper ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002212748 |
F |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Krüger, E et al. (2001) Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor. EMBO J. 20 852-63 PubMed GONUTS page
- ↑ () PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 3.4 3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
