ID   RSBW_STAEQ              Reviewed;         159 AA.
AC   Q5HMF0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=SERP1678;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW55034.1; -; Genomic_DNA.
DR   RefSeq; WP_001829903.1; NC_002976.3.
DR   AlphaFoldDB; Q5HMF0; -.
DR   SMR; Q5HMF0; -.
DR   STRING; 176279.SERP1678; -.
DR   EnsemblBacteria; AAW55034; AAW55034; SERP1678.
DR   GeneID; 50018230; -.
DR   KEGG; ser:SERP1678; -.
DR   eggNOG; COG2172; Bacteria.
DR   HOGENOM; CLU_090336_11_1_9; -.
DR   OMA; KPEYVGV; -.
DR   OrthoDB; 1832160at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..159
FT                   /note="Serine-protein kinase RsbW"
FT                   /id="PRO_0000203547"
SQ   SEQUENCE   159 AA;  17922 MW;  EA6A49C76218B78F CRC64;
     MQSTQDYIEM RLPASAEYVS LIRLTLSGVF SRAGASYDDI EDSKIAVSEA VTNAVKHAYK
     KNSEIGMINL CFEIFDDRIK IVISDQGESF DYEATKSHLG PYNDNENIDF LREGGLGLFL
     IESLMDEVTV YKESGVTISM IKYIKKEQVR NNGERVEIS