ID   RSBV_STAAR              Reviewed;         108 AA.
AC   Q6GF07;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Anti-sigma-B factor antagonist;
DE   AltName: Full=Anti-anti-sigma-B factor;
GN   Name=rsbV; OrderedLocusNames=SAR2154;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Positive regulator of sigma-B activity. Non-phosphorylated
CC       RsbV binds to RsbW, preventing its association with sigma-B. When
CC       phosphorylated, releases RsbW, which is then free to complex with and
CC       inactivate sigma-B (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by RsbW on a serine residue. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG41135.1; -; Genomic_DNA.
DR   RefSeq; WP_001052491.1; NC_002952.2.
DR   AlphaFoldDB; Q6GF07; -.
DR   SMR; Q6GF07; -.
DR   GeneID; 66840274; -.
DR   KEGG; sar:SAR2154; -.
DR   HOGENOM; CLU_115403_9_3_9; -.
DR   OMA; MNLAINI; -.
DR   OrthoDB; 1864829at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IEA:InterPro.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR003658; Anti-sigma_ant.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   TIGRFAMs; TIGR00377; ant_ant_sig; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein.
FT   CHAIN           1..108
FT                   /note="Anti-sigma-B factor antagonist"
FT                   /id="PRO_0000194191"
FT   DOMAIN          3..108
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   108 AA;  12205 MW;  461FC096E18D9AEE CRC64;
     MNLNIETTTQ DKFYEVKVGG ELDVYTVPEL EEVLTPMRQD GTRDIYVNLE NVSYMDSTGL
     GLFVGTLKAL NQNDKELYIL GVSDRIGRLF EITGLKDLMH VNEGTEVE