ID   SP2AB_BACHK             Reviewed;         146 AA.
AC   Q6HE93;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=BT9727_3814;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT61059.1; -; Genomic_DNA.
DR   RefSeq; WP_001243400.1; NC_005957.1.
DR   RefSeq; YP_038133.1; NC_005957.1.
DR   AlphaFoldDB; Q6HE93; -.
DR   SMR; Q6HE93; -.
DR   EnsemblBacteria; AAT61059; AAT61059; BT9727_3814.
DR   GeneID; 45023964; -.
DR   GeneID; 59155349; -.
DR   GeneID; 64199421; -.
DR   GeneID; 66266356; -.
DR   KEGG; btk:BT9727_3814; -.
DR   PATRIC; fig|281309.8.peg.4067; -.
DR   HOGENOM; CLU_090336_11_0_9; -.
DR   OMA; HAYEDKI; -.
DR   PRO; PR:Q6HE93; -.
DR   Proteomes; UP000001301; 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_0000203554"
SQ   SEQUENCE   146 AA;  16246 MW;  0A2A23B73908D55C CRC64;
     MRNEMNLQFS ALSQNESFAR VTVAAFIAQL DPTMEELTEI KTVVSEAVTN AIIHGYEGNA
     EGVVYISVIL EEAMVKLTIR DEGIGIFNLD EARQPLFTTK PELERSGMGF TIMENFMDEV
     EVISNESFGT TIHLTKYLSN SNALCN