ID   RSBW_STAA8              Reviewed;         159 AA.
AC   Q2FWJ3; O08077; P0A0H8; P95843; Q6XZ92; Q6XZ96;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 97.
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=SAOUHSC_02299;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9042755; DOI=10.1007/s002030050428;
RA   Kullik I., Giachino P.;
RT   "The alternative sigma factor sigmaB in Staphylococcus aureus: regulation
RT   of the sigB operon in response to growth phase and heat shock.";
RL   Arch. Microbiol. 167:151-159(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cramton S.E., Doering G.;
RT   "Role of sigB operon in Staphylococcus aureus biofilm formation.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD31333.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y07645; CAA68931.1; -; Genomic_DNA.
DR   EMBL; AY197751; AAP42788.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31333.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001190829.1; NZ_LS483365.1.
DR   RefSeq; YP_500777.1; NC_007795.1.
DR   AlphaFoldDB; Q2FWJ3; -.
DR   SMR; Q2FWJ3; -.
DR   STRING; 1280.SAXN108_2310; -.
DR   EnsemblBacteria; ABD31333; ABD31333; SAOUHSC_02299.
DR   GeneID; 3919170; -.
DR   KEGG; sao:SAOUHSC_02299; -.
DR   PATRIC; fig|93061.5.peg.2083; -.
DR   eggNOG; COG2172; Bacteria.
DR   HOGENOM; CLU_090336_11_1_9; -.
DR   PRO; PR:Q2FWJ3; -.
DR   Proteomes; UP000008816; 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_0000249338"
FT   CONFLICT        81
FT                   /note="I -> V (in Ref. 2; AAP42788)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   159 AA;  17921 MW;  57FA8EB8C1F9902B CRC64;
     MQSKEDFIEM RVPASAEYVS LIRLTLSGVF SRAGATYDDI EDAKIAVSEA VTNAVKHAYK
     ENNNVGIINI YFEILEDKIK IVISDKGDSF DYETTKSKIG PYDKDENIDF LREGGLGLFL
     IESLMDEVTV YKESGVTISM TKYIKKEQVR NNGERVEIS