RSBV_LISMO
ID RSBV_LISMO Reviewed; 114 AA.
AC P0A4J8; O85016;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Anti-sigma-B factor antagonist;
DE AltName: Full=Anti-anti-sigma-B factor;
GN Name=rsbV; OrderedLocusNames=lmo0893;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=689426;
RX PubMed=9658010; DOI=10.1128/jb.180.14.3650-3656.1998;
RA Wiedmann M., Arvik T.J., Hurley R.J., Boor K.J.;
RT "General stress transcription factor sigmaB and its role in acid tolerance
RT and virulence of Listeria monocytogenes.";
RL J. Bacteriol. 180:3650-3656(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AF032444; AAC38787.1; -; Genomic_DNA.
DR EMBL; AL591977; CAC98971.1; -; Genomic_DNA.
DR PIR; AE1186; AE1186.
DR RefSeq; NP_464419.1; NC_003210.1.
DR RefSeq; WP_003721460.1; NZ_CP023861.1.
DR AlphaFoldDB; P0A4J8; -.
DR SMR; P0A4J8; -.
DR STRING; 169963.lmo0893; -.
DR PaxDb; P0A4J8; -.
DR EnsemblBacteria; CAC98971; CAC98971; CAC98971.
DR GeneID; 61169907; -.
DR GeneID; 67409418; -.
DR GeneID; 986526; -.
DR KEGG; lmo:lmo0893; -.
DR PATRIC; fig|169963.11.peg.918; -.
DR eggNOG; COG1366; Bacteria.
DR HOGENOM; CLU_115403_9_3_9; -.
DR OMA; MNLAINI; -.
DR PhylomeDB; P0A4J8; -.
DR BioCyc; LMON169963:LMO0893-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0043856; F:anti-sigma factor antagonist activity; IBA:GO_Central.
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..114
FT /note="Anti-sigma-B factor antagonist"
FT /id="PRO_0000194187"
FT DOMAIN 4..114
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 114 AA; 12799 MW; AFCEEE64C146C023 CRC64;
MNISIEIKER DTDHIDIFVA GEIDAYTAPK VKEALEVYQV KEGIVLRIDL TEVSYMDSTG
LGVFVGAFKS LRQRQSELVL FGLSDRLFRL FEITGLSDII EIKNVEGEMN GNNA