ID   SP0A_CLOBU              Reviewed;         161 AA.
AC   P52937;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Stage 0 sporulation protein A homolog;
DE   Flags: Fragment;
GN   Name=spo0A;
OS   Clostridium butyricum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19398 / DSM 10702 / JCM 1391 / NCIMB 7423;
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 (By similarity).
CC       {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}.
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DR   EMBL; U09980; AAA18881.1; -; Unassigned_DNA.
DR   PIR; S60878; S60878.
DR   AlphaFoldDB; P52937; -.
DR   SMR; P52937; -.
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; 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..>161
FT                   /note="Stage 0 sporulation protein A homolog"
FT                   /id="PRO_0000081239"
FT   DOMAIN          <1..59
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        143..>161
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         161
SQ   SEQUENCE   161 AA;  18134 MW;  B1EB6BE1029FE1A2 CRC64;
     LGVLEKLNTM DLEKTPRIII LSAVGQDKIT QQAITLGADY YTVKPFDMEV FTKRIREMFN
     SAPTIQESSA QSNRVSYPTT SSYILTSEPK SKTPVDLETE ITNIIHEIGV PAHIKGYMYL
     REAITMVVND MELLSAVTKE LYPSIAKKYN TTASRVERAI R