SP2AB_ALKCK
ID SP2AB_ALKCK Reviewed; 146 AA.
AC Q5WH26;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=ABC1794;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD64329.1; -; Genomic_DNA.
DR RefSeq; WP_011246637.1; NC_006582.1.
DR AlphaFoldDB; Q5WH26; -.
DR SMR; Q5WH26; -.
DR STRING; 66692.ABC1794; -.
DR EnsemblBacteria; BAD64329; BAD64329; ABC1794.
DR KEGG; bcl:ABC1794; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_11_0_9; -.
DR OMA; HAYEDKI; -.
DR OrthoDB; 1832160at2; -.
DR Proteomes; UP000001168; 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..146
FT /note="Anti-sigma F factor"
FT /id="PRO_0000203559"
SQ SEQUENCE 146 AA; 16329 MW; B177E32742002DF9 CRC64;
MANKMNLAFS ALSENESFAR VTVSAFIAQL DPTMEELTEI KTIVSEAVTN AIIHGYENDP
NGQVYITAEL KDRELELIIR DEGVGISDLD EARQPLYTSK PELERSGMGF TIMENFCQEL
KVISEPMIGT TVYVKKQLTT TKAMCR