ID A0A1G8ISR2_9BACI Unreviewed; 163 AA.
AC A0A1G8ISR2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Serine-protein kinase RsbW {ECO:0000256|HAMAP-Rule:MF_00638};
DE EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_00638};
DE AltName: Full=Anti-sigma-B factor {ECO:0000256|HAMAP-Rule:MF_00638};
DE AltName: Full=Sigma-B negative effector RsbW {ECO:0000256|HAMAP-Rule:MF_00638};
GN Name=rsbW {ECO:0000256|HAMAP-Rule:MF_00638};
GN ORFNames=SAMN05216352_105328 {ECO:0000313|EMBL:SDI21949.1};
OS Alteribacillus bidgolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930129 {ECO:0000313|EMBL:SDI21949.1, ECO:0000313|Proteomes:UP000199017};
RN [1] {ECO:0000313|EMBL:SDI21949.1, ECO:0000313|Proteomes:UP000199017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4B,CCM 7963,CECT 7998,DSM 25260,IBRC-M 10614,KCTC 13821
RC {ECO:0000313|Proteomes:UP000199017};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|ARBA:ARBA00001433, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000775,
CC ECO:0000256|HAMAP-Rule:MF_00638};
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000256|ARBA:ARBA00037972, ECO:0000256|HAMAP-Rule:MF_00638}.
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DR EMBL; FNDU01000005; SDI21949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8ISR2; -.
DR STRING; 930129.SAMN05216352_105328; -.
DR OrthoDB; 9798941at2; -.
DR Proteomes; UP000199017; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 NCBIfam; TIGR01924; rsbW_low_gc; 1.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR PANTHER; PTHR35526:SF1; SERINE-PROTEIN KINASE RSBW; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00638};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00638, ECO:0000313|EMBL:SDI21949.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00638};
KW Reference proteome {ECO:0000313|Proteomes:UP000199017};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_00638};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00638}.
FT DOMAIN 13..140
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 163 AA; 17716 MW; 9B1194C841330288 CRC64;
MSDKAKDYIE MKLPAKAEYV GVVRLTVSGV ANRVGYSYDD IEDLKIAVAE ACTNVVDHAY
KQNGLMALGC SIYKDKIEIV VSDNGQSFNF DDLKKGLGPV DGTKPIGELE EGGLGLFLIN
SLMDKVEINR ESGVAIVMTK FLQRDEVEQD ANGVPAPTNA QKQ
//
