RSBW_LISW6
ID RSBW_LISW6 Reviewed; 157 AA.
AC A0AH12;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=lwe0876;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK20294.1; -; Genomic_DNA.
DR RefSeq; WP_011701709.1; NC_008555.1.
DR AlphaFoldDB; A0AH12; -.
DR SMR; A0AH12; -.
DR STRING; 386043.lwe0876; -.
DR EnsemblBacteria; CAK20294; CAK20294; lwe0876.
DR GeneID; 61188764; -.
DR KEGG; lwe:lwe0876; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_11_1_9; -.
DR OMA; KPEYVGV; -.
DR OrthoDB; 1832160at2; -.
DR Proteomes; UP000000779; 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; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..157
FT /note="Serine-protein kinase RsbW"
FT /id="PRO_0000301408"
SQ SEQUENCE 157 AA; 17538 MW; 79CE9F2826906223 CRC64;
MATTHDKITL QLPAKPEYVS LGRLSLSGIA SRAGFSYEAI EDLKIAVSEA ITNSVKHAFK
GEEDGEIIVE YLIYEDKLEV RVSDNGTSFD LESRKQEIGP YEVDEDAEMM RIGGLGLFLI
ETLMDDVKLY YDEGVSVVMT KYINEKQVEE NAKSIST