ID   RSBV_STAEQ              Reviewed;         108 AA.
AC   Q5HME9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Anti-sigma-B factor antagonist;
DE   AltName: Full=Anti-anti-sigma-B factor;
GN   Name=rsbV; OrderedLocusNames=SERP1679;
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: 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; CP000029; AAW55035.1; -; Genomic_DNA.
DR   RefSeq; WP_001829952.1; NC_002976.3.
DR   AlphaFoldDB; Q5HME9; -.
DR   SMR; Q5HME9; -.
DR   STRING; 176279.SERP1679; -.
DR   EnsemblBacteria; AAW55035; AAW55035; SERP1679.
DR   GeneID; 50018229; -.
DR   KEGG; ser:SERP1679; -.
DR   eggNOG; COG1366; Bacteria.
DR   HOGENOM; CLU_115403_9_3_9; -.
DR   OMA; MNLAINI; -.
DR   OrthoDB; 1864829at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..108
FT                   /note="Anti-sigma-B factor antagonist"
FT                   /id="PRO_0000194197"
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;  12093 MW;  DE3C2F0EC160D1B9 CRC64;
     MNLNIETITH DDFYEVKVGG ELDVYTVPEL EEVLVPMRQE GTHDVHVNLA NVSYMDSTGL
     GLFVGTLKAL NQNDKNLYIL GVSERIGRLF DITGLKDLMH VNEGTEVE