ID A0A495AGC0_9BACI Unreviewed; 146 AA.
AC A0A495AGC0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Anti-sigma F factor {ECO:0000256|HAMAP-Rule:MF_00637};
DE EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_00637};
DE AltName: Full=Stage II sporulation protein AB {ECO:0000256|HAMAP-Rule:MF_00637};
GN Name=spoIIAB {ECO:0000256|HAMAP-Rule:MF_00637};
GN ORFNames=D8M06_02615 {ECO:0000313|EMBL:RKQ37715.1};
OS Oceanobacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ37715.1, ECO:0000313|Proteomes:UP000269301};
RN [1] {ECO:0000313|EMBL:RKQ37715.1, ECO:0000313|Proteomes:UP000269301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ37715.1,
RC ECO:0000313|Proteomes:UP000269301};
RX PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT bacterium from a hypersaline lake.";
RL Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
CC -!- FUNCTION: Binds to sigma F and blocks its ability to form an RNA
CC polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine
CC residue. This phosphorylation may enable SpoIIAA to act as an anti-
CC anti-sigma factor that counteracts SpoIIAB and thus releases sigma F
CC from inhibition. {ECO:0000256|HAMAP-Rule:MF_00637}.
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_00637};
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_00637};
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000256|ARBA:ARBA00037972, ECO:0000256|HAMAP-Rule:MF_00637}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKQ37715.1}.
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DR EMBL; RBZP01000001; RKQ37715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495AGC0; -.
DR OrthoDB; 9768808at2; -.
DR Proteomes; UP000269301; 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:0030436; P:asexual sporulation; IEA:UniProtKB-UniRule.
DR GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00637; Anti_sigma_F; 1.
DR InterPro; IPR010194; Anti-sigma_F.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR NCBIfam; TIGR01925; spIIAB; 1.
DR PANTHER; PTHR35526:SF7; ANTI-SIGMA F FACTOR; 1.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SMART; SM00387; HATPase_c; 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_00637};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00637};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00637};
KW Reference proteome {ECO:0000313|Proteomes:UP000269301};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_00637};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969, ECO:0000256|HAMAP-
KW Rule:MF_00637};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00637, ECO:0000313|EMBL:RKQ37715.1}.
FT DOMAIN 35..140
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 146 AA; 16245 MW; 22EBA127B309ABCA CRC64;
MRNEMVVEFS SISENEAFAR VTVGAFITQL DPTMDELTEI KTVVSEAVTN AIIHGYNNEP
DHKIKIKCVI DNGEIELIIQ DTGIGIGDIE KARQPLYTSK PELERSGMGF TIIENFMDSV
KVTSSPTEGT KLCMKKQLVK SKTVYN
//
