RSBW_BACAN
ID RSBW_BACAN Reviewed; 160 AA.
AC Q9K5J7; Q6I2H9; Q6KWA7;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
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};
GN OrderedLocusNames=BA_0991, GBAA_0991, BAS0927;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=9131;
RX PubMed=10960085; DOI=10.1128/jb.182.18.5036-5045.2000;
RA Fouet A., Namy O., Lambert G.;
RT "Characterization of the operon encoding the alternative sigma(B) factor
RT from Bacillus anthracis and its role in virulence.";
RL J. Bacteriol. 182:5036-5045(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB95033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ272497; CAB95033.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE016879; AAP24978.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30094.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53252.1; -; Genomic_DNA.
DR RefSeq; NP_843492.1; NC_003997.3.
DR RefSeq; WP_000970578.1; NZ_WXXJ01000020.1.
DR RefSeq; YP_027201.1; NC_005945.1.
DR AlphaFoldDB; Q9K5J7; -.
DR SMR; Q9K5J7; -.
DR IntAct; Q9K5J7; 1.
DR STRING; 261594.GBAA_0991; -.
DR DNASU; 1088183; -.
DR EnsemblBacteria; AAP24978; AAP24978; BA_0991.
DR EnsemblBacteria; AAT30094; AAT30094; GBAA_0991.
DR GeneID; 45021033; -.
DR KEGG; ban:BA_0991; -.
DR KEGG; bar:GBAA_0991; -.
DR KEGG; bat:BAS0927; -.
DR PATRIC; fig|198094.11.peg.982; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_11_1_9; -.
DR OMA; KPEYVGV; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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..160
FT /note="Serine-protein kinase RsbW"
FT /id="PRO_0000203525"
SQ SEQUENCE 160 AA; 18241 MW; 20DC9C9185E887AA CRC64;
MMERFEKIEM KIPAKAEYVA IIRLTMAGVA NRMGFAYDDI EDMKIAISEA CTNIVQHAYK
EDVGEIAIVF GLYENRLEIM VADNGVSFDF NNLRSKVGPY DISKPVEHLP ENGLGLYLIN
TLMDDIQIMH DEGMTVLMTK YIQREQVEND GNPISTYESY
