ID   RSBV_STAES              Reviewed;         108 AA.
AC   P0C0Q8; Q8VSV6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-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=SE_1670;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05269.1; -; Genomic_DNA.
DR   RefSeq; NP_765225.1; NC_004461.1.
DR   RefSeq; WP_001829952.1; NZ_WBME01000071.1.
DR   AlphaFoldDB; P0C0Q8; -.
DR   SMR; P0C0Q8; -.
DR   STRING; 176280.SE_1670; -.
DR   EnsemblBacteria; AAO05269; AAO05269; SE_1670.
DR   GeneID; 50018229; -.
DR   KEGG; sep:SE_1670; -.
DR   PATRIC; fig|176280.10.peg.1631; -.
DR   eggNOG; COG1366; Bacteria.
DR   HOGENOM; CLU_115403_9_3_9; -.
DR   OMA; MNLAINI; -.
DR   Proteomes; UP000001411; 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_0000194196"
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