RSBV_STAAS
ID RSBV_STAAS Reviewed; 108 AA.
AC Q6G7P3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Anti-sigma-B factor antagonist;
DE AltName: Full=Anti-anti-sigma-B factor;
GN Name=rsbV; OrderedLocusNames=SAS1971;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571857; CAG43778.1; -; Genomic_DNA.
DR RefSeq; WP_001052491.1; NC_002953.3.
DR AlphaFoldDB; Q6G7P3; -.
DR SMR; Q6G7P3; -.
DR GeneID; 66840274; -.
DR KEGG; sas:SAS1971; -.
DR HOGENOM; CLU_115403_9_3_9; -.
DR OMA; MNLAINI; -.
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_0000194192"
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