ID   SP0A_BACTU              Reviewed;         264 AA.
AC   P0A4I4; P52935;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Stage 0 sporulation protein A;
GN   Name=spo0A;
OS   Bacillus thuringiensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=407;
RX   PubMed=9634751; DOI=10.1038/nbt0195-67;
RA   Lereclus D., Agaisse H., Gominet M., Chaufaux J.;
RT   "Overproduction of encapsulated insecticidal crystal proteins in a Bacillus
RT   thuringiensis spo0A mutant.";
RL   Biotechnology (N.Y.) 13:67-71(1995).
CC   -!- FUNCTION: May play the central regulatory role in sporulation. It may
CC       be an element of the effector pathway responsible for the activation of
CC       sporulation genes in response to nutritional stress. Spo0A may act in
CC       concert with Spo0H (a sigma factor) to control the expression of some
CC       genes that are critical to the sporulation process. Repressor of abrB,
CC       activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3'
CC       (0A box) (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by KinA and KinB. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X80639; CAA56683.1; -; Genomic_DNA.
DR   PIR; S47062; S47062.
DR   RefSeq; WP_011110369.1; NZ_WBOO01000003.1.
DR   AlphaFoldDB; P0A4I4; -.
DR   SMR; P0A4I4; -.
DR   GeneID; 67508809; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0051606; P:detection of stimulus; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR014879; Spo0A_C.
DR   InterPro; IPR012052; Spore_0_A.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF08769; Spo0A_C; 1.
DR   PIRSF; PIRSF002937; Res_reg_Spo0A; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   TIGRFAMs; TIGR02875; spore_0_A; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; Calcium; Cytoplasm; DNA-binding; Metal-binding; Phosphoprotein;
KW   Repressor; Sporulation; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..264
FT                   /note="Stage 0 sporulation protein A"
FT                   /id="PRO_0000081235"
FT   DOMAIN          5..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        196..215
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   BINDING         10
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   264 AA;  29415 MW;  9A2B331EE36EFFBE CRC64;
     MEKIKVCLVD DNKELVSMLE SYVAAQDDME VIGTAYNGQE CLNLLTDKQP DVLVLDIIMP
     HLDGLAVLEK MRHIERLKQP SVIMLTAFGQ EDVTKKAVDL GASYFILKPF DMENLTSHIR
     QVSGKANAMI KRPLPSFRSA TTVDGKPKNL DASITSIIHE IGVPAHIKGY MYLREAISMV
     YNDIELLGSI TKVLYPDIAK KYNTTASRVE RAIRHAIEVA WSRGNIDSIS SLFGYTVSMS
     KAKPTNSEFI AMVADKLRLE HKAS