ID   SP2AB_GEOTN             Reviewed;         146 AA.
AC   A4IQI5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Anti-sigma F factor {ECO:0000255|HAMAP-Rule:MF_00637};
DE            EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_00637};
DE   AltName: Full=Stage II sporulation protein AB {ECO:0000255|HAMAP-Rule:MF_00637};
GN   Name=spoIIAB {ECO:0000255|HAMAP-Rule:MF_00637};
GN   OrderedLocusNames=GTNG_2240;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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:0000255|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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00637};
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC       {ECO:0000255|HAMAP-Rule:MF_00637}.
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DR   EMBL; CP000557; ABO67589.1; -; Genomic_DNA.
DR   RefSeq; WP_008879718.1; NC_009328.1.
DR   AlphaFoldDB; A4IQI5; -.
DR   SMR; A4IQI5; -.
DR   STRING; 420246.GTNG_2240; -.
DR   EnsemblBacteria; ABO67589; ABO67589; GTNG_2240.
DR   KEGG; gtn:GTNG_2240; -.
DR   eggNOG; COG2172; Bacteria.
DR   HOGENOM; CLU_090336_11_0_9; -.
DR   OMA; HAYEDKI; -.
DR   OrthoDB; 1832160at2; -.
DR   Proteomes; UP000001578; 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: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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 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   Pfam; PF13581; HATPase_c_2; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01925; spIIAB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Sporulation; Transferase.
FT   CHAIN           1..146
FT                   /note="Anti-sigma F factor"
FT                   /id="PRO_0000301414"
SQ   SEQUENCE   146 AA;  16168 MW;  CBFD731E17347F7E CRC64;
     MRNEMHLQFS ARSENESFAR VTVAAFVAQL DPTIDELTEI KTVVSEAVTN AIIHGYNNDP
     NGIVFISVVI EDGIVHLTVR DEGVGIANID EARQPLFTTK PELERSGMGF TIMENFMDEV
     VVESEVNKGT TVYLKKHIAK SKALCN