(data stored in SCRATCH zone)

SWISSPROT: D6XY01_BACIE

ID   D6XY01_BACIE            Unreviewed;       165 AA.
AC   D6XY01;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Serine-protein kinase RsbW {ECO:0000256|HAMAP-Rule:MF_00638};
DE            EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_00638};
DE   AltName: Full=Anti-sigma-B factor {ECO:0000256|HAMAP-Rule:MF_00638};
DE   AltName: Full=Sigma-B negative effector RsbW {ECO:0000256|HAMAP-Rule:MF_00638};
GN   Name=rsbW {ECO:0000256|HAMAP-Rule:MF_00638};
GN   OrderedLocusNames=Bsel_0538 {ECO:0000313|EMBL:ADH98074.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98074.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98074.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negative regulator of sigma-B activity. Phosphorylates
CC       and inactivates its specific antagonist protein, RsbV. Upon
CC       phosphorylation of RsbV, RsbW is released and binds to sigma-B,
CC       thereby blocking its ability to form an RNA polymerase holoenzyme
CC       (E-sigma-B). {ECO:0000256|HAMAP-Rule:MF_00638}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00638};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00638};
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC       {ECO:0000256|HAMAP-Rule:MF_00638}.
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DR   EMBL; CP001791; ADH98074.1; -; Genomic_DNA.
DR   RefSeq; WP_013171503.1; NC_014219.1.
DR   STRING; 439292.Bsel_0538; -.
DR   EnsemblBacteria; ADH98074; ADH98074; Bsel_0538.
DR   KEGG; bse:Bsel_0538; -.
DR   eggNOG; COG2172; LUCA.
DR   HOGENOM; HOG000269932; -.
DR   KO; K04757; -.
DR   OMA; KPEYVGV; -.
DR   OrthoDB; 1832160at2; -.
DR   BioCyc; BSEL439292:G1GLR-566-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00638; Anti_sigma_B; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010193; RsbW.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01924; rsbW_low_gc; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XY01.
DR   SWISS-2DPAGE; D6XY01.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00638};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00638, ECO:0000313|EMBL:ADH98074.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00638};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_00638,
KW   ECO:0000313|EMBL:ADH98074.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00638,
KW   ECO:0000313|EMBL:ADH98074.1}.
FT   DOMAIN       12    144       HATPase_c. {ECO:0000259|Pfam:PF13581}.
SQ   SEQUENCE   165 AA;  18264 MW;  29DE5263DFE84D1C CRC64;
     MSKVADRIEM NVPAKAEYVG VVRLTASGVA NRLGYSYDDI EDIKLAVAEA CTNVVNHAYE
     KADDEVSHDI HLKFSVYEDR MEFVIADQGG AVDLDVLKKK RGPLNASQAI EDMKEGGLGL
     FLIETLMDEV DIQGDTGVII TMTKFLKRDE VEPGDERTSE ELPKQ
//

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