ID   RSBW_STAAC              Reviewed;         159 AA.
AC   Q5HED6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Serine-protein kinase RsbW;
DE            EC=2.7.11.1;
DE   AltName: Full=Anti-sigma-B factor;
DE   AltName: Full=Sigma-B negative effector RsbW;
GN   Name=rsbW; OrderedLocusNames=SACOL2055;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8830703; DOI=10.1128/jb.178.20.6036-6042.1996;
RA   Wu S.-W., de Lencastre H., Tomasz A.;
RT   "Sigma-B, a putative operon encoding alternate sigma factor of
RT   Staphylococcus aureus RNA polymerase: molecular cloning and DNA
RT   sequencing.";
RL   J. Bacteriol. 178:6036-6042(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
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) (By
CC       similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor family. {ECO:0000305}.
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DR   EMBL; Y09929; CAA71067.1; -; Genomic_DNA.
DR   EMBL; CP000046; AAW37017.1; -; Genomic_DNA.
DR   RefSeq; WP_001190829.1; NC_002951.2.
DR   AlphaFoldDB; Q5HED6; -.
DR   SMR; Q5HED6; -.
DR   EnsemblBacteria; AAW37017; AAW37017; SACOL2055.
DR   KEGG; sac:SACOL2055; -.
DR   HOGENOM; CLU_090336_11_1_9; -.
DR   OMA; KPEYVGV; -.
DR   Proteomes; UP000000530; 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_0000203539"
SQ   SEQUENCE   159 AA;  17921 MW;  57FA8EB8C1F9902B CRC64;
     MQSKEDFIEM RVPASAEYVS LIRLTLSGVF SRAGATYDDI EDAKIAVSEA VTNAVKHAYK
     ENNNVGIINI YFEILEDKIK IVISDKGDSF DYETTKSKIG PYDKDENIDF LREGGLGLFL
     IESLMDEVTV YKESGVTISM TKYIKKEQVR NNGERVEIS