ID   SP2AB_CALS4             Reviewed;         143 AA.
AC   Q8RAA8;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
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}; OrderedLocusNames=TTE1316;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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; AE008691; AAM24540.1; -; Genomic_DNA.
DR   RefSeq; WP_011025623.1; NC_003869.1.
DR   AlphaFoldDB; Q8RAA8; -.
DR   SMR; Q8RAA8; -.
DR   STRING; 273068.TTE1316; -.
DR   EnsemblBacteria; AAM24540; AAM24540; TTE1316.
DR   KEGG; tte:TTE1316; -.
DR   eggNOG; COG2172; Bacteria.
DR   HOGENOM; CLU_090336_11_0_9; -.
DR   OMA; HAYEDKI; -.
DR   OrthoDB; 1832160at2; -.
DR   Proteomes; UP000000555; 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..143
FT                   /note="Anti-sigma F factor"
FT                   /id="PRO_0000203569"
SQ   SEQUENCE   143 AA;  16117 MW;  CF3582C837C1AC76 CRC64;
     MEYNNMMELK FLSKSQNESF ARTVVAAFAA QLDPTIEEIA DIKTAVSEAV TNCIIHAYEN
     KIGIITIRAF ILDNKITIEV IDEGKGIEDV EKAMQPLFTT RLEEERAGMG FTVMQTFMDE
     LEVESTPGKG TLVRMTKYIG RNR