RSBW_STAEP
ID RSBW_STAEP Reviewed; 159 AA.
AC P0C0M6; Q8VSV5; Q9F7V2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Clinical isolate 1457;
RX PubMed=11274123; DOI=10.1128/jb.183.8.2624-2633.2001;
RA Knobloch J.K.-M., Bartscht K., Sabottke A., Rohde H., Feucht H.-H.,
RA Mack D.;
RT "Biofilm formation by Staphylococcus epidermidis depends on functional
RT rsbU, an activator of the sigB operon: differential activation mechanisms
RT due to ethanol and salt stress.";
RL J. Bacteriol. 183:2624-2633(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11705980; DOI=10.1128/iai.69.12.7933-7936.2001;
RA Kies S., Otto M., Vuong C., Gotz F.;
RT "Identification of the sigB operon in Staphylococcus epidermidis:
RT construction and characterization of a sigB deletion mutant.";
RL Infect. Immun. 69:7933-7936(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; AF274004; AAG23812.1; -; Genomic_DNA.
DR EMBL; AF359562; AAL37942.1; -; Genomic_DNA.
DR RefSeq; WP_001829903.1; NZ_WLVA01000001.1.
DR AlphaFoldDB; P0C0M6; -.
DR SMR; P0C0M6; -.
DR GeneID; 50018230; -.
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..159
FT /note="Serine-protein kinase RsbW"
FT /id="PRO_0000203545"
FT CONFLICT 81
FT /note="I -> V (in Ref. 2; AAL37942)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> S (in Ref. 2; AAL37942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 17922 MW; EA6A49C76218B78F CRC64;
MQSTQDYIEM RLPASAEYVS LIRLTLSGVF SRAGASYDDI EDSKIAVSEA VTNAVKHAYK
KNSEIGMINL CFEIFDDRIK IVISDQGESF DYEATKSHLG PYNDNENIDF LREGGLGLFL
IESLMDEVTV YKESGVTISM IKYIKKEQVR NNGERVEIS
