ID   SP2AB_CLOTE             Reviewed;         141 AA.
AC   P59623; Q891W6;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=CTC_02247;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36729.1; -; Genomic_DNA.
DR   RefSeq; WP_011100390.1; NC_004557.1.
DR   AlphaFoldDB; P59623; -.
DR   SMR; P59623; -.
DR   STRING; 212717.CTC_02247; -.
DR   EnsemblBacteria; AAO36729; AAO36729; CTC_02247.
DR   GeneID; 64179676; -.
DR   KEGG; ctc:CTC_02247; -.
DR   HOGENOM; CLU_090336_11_0_9; -.
DR   OMA; HAYEDKI; -.
DR   OrthoDB; 1832160at2; -.
DR   Proteomes; UP000001412; 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; Reference proteome;
KW   Serine/threonine-protein kinase; Sporulation; Transferase.
FT   CHAIN           1..141
FT                   /note="Anti-sigma F factor"
FT                   /id="PRO_0000203564"
SQ   SEQUENCE   141 AA;  15888 MW;  D97464725A7112FC CRC64;
     MFDNMMKLEI LSKSENESFA RATVAAFASQ LDPTLNELTD IKTAVSEAVT NSIIHGYENK
     GDKTVKIEAY IKDKELTVII WDEGIGIENV NLAMQPLYTS RPDLERSGMG FTVMQSFMDE
     LEVKSEKNKG TKIIMKKIFN N