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BACSU:MCSB

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Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) mcsB (ECO:0000255 with HAMAP-Rule:MF_00602) (synonyms: yacI)
Protein Name(s) Protein-arginine kinase (ECO:0000255 with HAMAP-Rule:MF_00602)
External Links
UniProt P37570
EMBL D26185
AL009126
U02604
PIR S66114
RefSeq NP_387966.1
WP_003235007.1
ProteinModelPortal P37570
SMR P37570
IntAct P37570
MINT MINT-4789055
STRING 224308.Bsubs1_010100000440
PaxDb P37570
EnsemblBacteria CAB11861
GeneID 936939
KEGG bsu:BSU00850
PATRIC 18971675
eggNOG ENOG41066A3
COG3869
HOGENOM HOG000082112
InParanoid P37570
KO K19405
OMA IIMQERV
OrthoDB EOG6NKR1D
PhylomeDB P37570
BioCyc BSUB:BSU00850-MONOMER
Proteomes UP000001570
GO GO:0005737
GO:0005524
GO:0016775
GO:0004672
Gene3D 3.30.590.10
HAMAP MF_00602
InterPro IPR023660
IPR000749
IPR022415
IPR022414
IPR014746
PANTHER PTHR11547
Pfam PF00217
PROSITE PS00112
PS51510

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006508

proteolysis

PMID:11179229[1]

ECO:0000315

P

McsB play a role in regulating transcription of CtsR-dependent heat shock genes. Figure 5- In the mcsB mutants, CtsR-dependent heat shock proteins under non-stressed conditions were increased when compared with the wild-type. McsB influences the CtsR-mediated repression negatively. Figure 6B- The half-life of the CtsR repressor was increased in McsB mutants, suggesting that McsB destabilizes CtsR.

complete
CACAO 11545

enables

GO:0016301

kinase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:88407
MGI:MGI:88413
PANTHER:PTN000167125
RGD:2358
RGD:61976
UniProtKB:P00565
UniProtKB:P05122

F

Seeded From UniProt

complete

GO:0006508

proteolysis

PMID:11179229[1]

ECO:0000314

P

Through gel mobility shift experiments (Figure 6, lanes 8-10), it was shown that addition of McsB to CtsR led to a decrease in the amount of DNA retarded by CtsR. This suests that McsB can remove the DNA binding capacity of CtsR.

complete
CACAO 11546

involved_in

GO:0006468

protein phosphorylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004672

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014746

F

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022414
InterPro:IPR022415

F

Seeded From UniProt

complete

enables

GO:0016772

transferase activity, transferring phosphorus-containing groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000749
InterPro:IPR022414
InterPro:IPR022415

F

Seeded From UniProt

complete

enables

GO:0016775

phosphotransferase activity, nitrogenous group as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023660

F

Seeded From UniProt

complete

enables

GO:0004672

protein kinase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000098157

F

Seeded From UniProt

complete

enables

GO:0016775

phosphotransferase activity, nitrogenous group as acceptor

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000098157

F

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 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
  2. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page