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SP2AB_BACLD
ID   SP2AB_BACLD             Reviewed;         146 AA.
AC   Q65HU3; Q62T93;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=BLi02496, BL00777;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU41371.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU24016.1; -; Genomic_DNA.
DR   RefSeq; WP_009327954.1; NC_006322.1.
DR   AlphaFoldDB; Q65HU3; -.
DR   SMR; Q65HU3; -.
DR   STRING; 279010.BL00777; -.
DR   EnsemblBacteria; AAU24016; AAU24016; BL00777.
DR   KEGG; bld:BLi02496; -.
DR   KEGG; bli:BL00777; -.
DR   eggNOG; COG2172; Bacteria.
DR   HOGENOM; CLU_090336_11_0_9; -.
DR   OMA; HAYEDKI; -.
DR   OrthoDB; 1832160at2; -.
DR   BioCyc; BLIC279010:BLI_RS12360-MON; -.
DR   Proteomes; UP000000606; 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_0000203556"
SQ   SEQUENCE   146 AA;  16198 MW;  E21BEBC6080524BB CRC64;
     MKNEMNIQFT ALSQNESFAR VTVAAFIAQL DPTMDELTEI KTVVSEAVTN AIIHGYENSG
     QGNVYISVTL EDHIVYLTIR DEGVGIPNLE EARQPLFTTK PELERSGMGF TIMENFMDDI
     SIDSSPEMGT TIHLTKHLSK SKALCN
 
 
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