ID   RSBW_STAES              Reviewed;         159 AA.
AC   P0C0M7; Q8VSV5; Q9F7V2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine-protein kinase RsbW {ECO:0000255|HAMAP-Rule:MF_00638};
DE            EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_00638};
DE   AltName: Full=Anti-sigma-B factor {ECO:0000255|HAMAP-Rule:MF_00638};
DE   AltName: Full=Sigma-B negative effector RsbW {ECO:0000255|HAMAP-Rule:MF_00638};
GN   Name=rsbW {ECO:0000255|HAMAP-Rule:MF_00638}; OrderedLocusNames=SE_1669;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Negative regulator of sigma-B activity. Phosphorylates and
CC       inactivates its specific antagonist protein, RsbV. Upon phosphorylation
CC       of RsbV, RsbW is released and binds to sigma-B, thereby blocking its
CC       ability to form an RNA polymerase holoenzyme (E-sigma-B).
CC       {ECO:0000255|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, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00638};
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC       {ECO:0000255|HAMAP-Rule:MF_00638}.
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DR   EMBL; AE015929; AAO05268.1; -; Genomic_DNA.
DR   RefSeq; NP_765224.1; NC_004461.1.
DR   RefSeq; WP_001829903.1; NZ_WBME01000071.1.
DR   AlphaFoldDB; P0C0M7; -.
DR   SMR; P0C0M7; -.
DR   STRING; 176280.SE_1669; -.
DR   EnsemblBacteria; AAO05268; AAO05268; SE_1669.
DR   GeneID; 50018230; -.
DR   KEGG; sep:SE_1669; -.
DR   PATRIC; fig|176280.10.peg.1630; -.
DR   eggNOG; COG2172; Bacteria.
DR   HOGENOM; CLU_090336_11_1_9; -.
DR   OMA; KPEYVGV; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..159
FT                   /note="Serine-protein kinase RsbW"
FT                   /id="PRO_0000203546"
SQ   SEQUENCE   159 AA;  17922 MW;  EA6A49C76218B78F CRC64;
     MQSTQDYIEM RLPASAEYVS LIRLTLSGVF SRAGASYDDI EDSKIAVSEA VTNAVKHAYK
     KNSEIGMINL CFEIFDDRIK IVISDQGESF DYEATKSHLG PYNDNENIDF LREGGLGLFL
     IESLMDEVTV YKESGVTISM IKYIKKEQVR NNGERVEIS