RSBW_LISMO
ID RSBW_LISMO Reviewed; 157 AA.
AC Q8Y8K6; O88131;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Serine-protein kinase RsbW {ECO:0000255|HAMAP-Rule:MF_00638};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_00638};
DE AltName: Full=Anti-sigma-B factor {ECO:0000255|HAMAP-Rule:MF_00638};
DE AltName: Full=Sigma-B negative effector RsbW {ECO:0000255|HAMAP-Rule:MF_00638};
GN Name=rsbW {ECO:0000255|HAMAP-Rule:MF_00638}; OrderedLocusNames=lmo0894;
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=LO4035;
RX PubMed=9721294; DOI=10.1128/jb.180.17.4547-4554.1998;
RA Becker L.A., Cetin M.S., Hutkins R.W., Benson A.K.;
RT "Identification of the gene encoding the alternative sigma factor sigmaB
RT from Listeria monocytogenes and its role in osmotolerance.";
RL J. Bacteriol. 180:4547-4554(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ferreira A., Gray M.J., Wiedmann M., Boor K.J.;
RT "Comparative genomic analyses of the sigB operon in Gram-positive
RT bacteria.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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: Negative regulator of sigma-B activity. Phosphorylates and
CC inactivates its specific antagonist protein, RsbV. Upon phosphorylation
CC of RsbV, RsbW is released and binds to sigma-B, thereby blocking its
CC ability to form an RNA polymerase holoenzyme (E-sigma-B).
CC {ECO:0000255|HAMAP-Rule:MF_00638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00638};
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000255|HAMAP-Rule:MF_00638}.
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DR EMBL; AL591977; CAC98972.1; -; Genomic_DNA.
DR EMBL; AF074855; AAC34826.1; -; Genomic_DNA.
DR EMBL; AF032444; AAC38788.1; -; Genomic_DNA.
DR EMBL; AY156593; AAN75463.1; -; Genomic_DNA.
DR PIR; AF1186; AF1186.
DR RefSeq; NP_464420.1; NC_003210.1.
DR RefSeq; WP_003721461.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y8K6; -.
DR SMR; Q8Y8K6; -.
DR STRING; 169963.lmo0894; -.
DR PaxDb; Q8Y8K6; -.
DR EnsemblBacteria; CAC98972; CAC98972; CAC98972.
DR GeneID; 67409417; -.
DR GeneID; 986524; -.
DR KEGG; lmo:lmo0894; -.
DR PATRIC; fig|169963.11.peg.919; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_11_1_9; -.
DR OMA; KPEYVGV; -.
DR PhylomeDB; Q8Y8K6; -.
DR BioCyc; LMON169963:LMO0894-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00638; Anti_sigma_B; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010193; RsbW.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR01924; rsbW_low_gc; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..157
FT /note="Serine-protein kinase RsbW"
FT /id="PRO_0000203535"
FT VARIANT 63
FT /note="E -> D (in strain: 689426 and LO4035)"
FT VARIANT 102
FT /note="D -> E (in strain: 689426 and LO4035)"
SQ SEQUENCE 157 AA; 17498 MW; FDAFA0C442C6359A CRC64;
MATMHDKITL QLPAKPEYVS LGRLSLSGIA SRAGFSYEAI EDLKIAVSEA ITNSVKHAFK
GEEDGEITVE YLIYEDKLEV RVSDNGTSFD LETRKQEIGP YDVGEDAEMM RIGGLGLFLI
ETLMDDVKLY YDEGVSVVMT KYINEKQVEE NAKSIST
