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Database: UniProt
Entry: RSBV_STAA8
LinkDB: RSBV_STAA8
Original site: RSBV_STAA8 
ID   RSBV_STAA8              Reviewed;         108 AA.
AC   P60070; O05343; P95842; Q2FWJ2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Anti-sigma-B factor antagonist;
DE   AltName: Full=Anti-anti-sigma-B factor;
GN   Name=rsbV; OrderedLocusNames=SAOUHSC_02300;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; 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 [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: 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; Y07645; CAA68930.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31334.1; -; Genomic_DNA.
DR   RefSeq; WP_001052491.1; NZ_LS483365.1.
DR   RefSeq; YP_500778.1; NC_007795.1.
DR   AlphaFoldDB; P60070; -.
DR   SMR; P60070; -.
DR   STRING; 93061.SAOUHSC_02300; -.
DR   PaxDb; 1280-SAXN108_2311; -.
DR   GeneID; 3919171; -.
DR   GeneID; 66840274; -.
DR   KEGG; sao:SAOUHSC_02300; -.
DR   PATRIC; fig|93061.5.peg.2084; -.
DR   eggNOG; COG1366; Bacteria.
DR   HOGENOM; CLU_115403_9_3_9; -.
DR   OrthoDB; 9793697at2; -.
DR   PRO; PR:P60070; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IBA:GO_Central.
DR   CDD; cd07043; STAS_anti-anti-sigma_factors; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR003658; Anti-sigma_ant.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR00377; ant_ant_sig; 1.
DR   PANTHER; PTHR33495; ANTI-SIGMA FACTOR ANTAGONIST TM_1081-RELATED-RELATED; 1.
DR   PANTHER; PTHR33495:SF9; ANTI-SIGMA-B FACTOR ANTAGONIST; 1.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 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_0000194194"
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
//
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