ID   SP0A_BACCE              Reviewed;         150 AA.
AC   P52930;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Stage 0 sporulation protein A;
DE   Flags: Fragment;
GN   Name=spo0A;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10876 / DSM 9378 / NRRL B-569;
RX   PubMed=7885226; DOI=10.1111/j.1365-2958.1994.tb02176.x;
RA   Brown D.P., Ganova-Raeva L., Green B.D., Wilkinson S.R., Young M.,
RA   Youngman P.;
RT   "Characterization of spo0A homologues in diverse Bacillus and Clostridium
RT   species identifies a probable DNA-binding domain.";
RL   Mol. Microbiol. 14:411-426(1994).
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}.
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DR   EMBL; U09972; AAA18873.1; -; Unassigned_DNA.
DR   PIR; S60870; S60870.
DR   AlphaFoldDB; P52930; -.
DR   SMR; P52930; -.
DR   STRING; 1396.DJ87_691; -.
DR   eggNOG; COG0745; Bacteria.
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   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; Phosphoprotein; Repressor;
KW   Sporulation; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           <1..>150
FT                   /note="Stage 0 sporulation protein A"
FT                   /id="PRO_0000081227"
FT   DOMAIN          <1..59
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        132..>150
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         150
SQ   SEQUENCE   150 AA;  16844 MW;  17E977501F151D35 CRC64;
     LAVLEKMRHI ERLKQPSVIM LTAFGQEDVT KKAVDLGASY FILKPFDMEN LPSHIRQVSG
     KANTMIKRPL PSFRSATTVD GKPKNLDASI TSIIHEIGVP AHIKGYMYLR EAISMVYNDI
     ELLGSITKVL YPDIAKKYNT TASRVERAIR