ID   SP0A_CLOB8              Reviewed;         273 AA.
AC   P52936; A6LU54;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Stage 0 sporulation protein A homolog;
GN   Name=spo0A; OrderedLocusNames=Cbei_1712;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-223.
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; CP000721; ABR33884.1; -; Genomic_DNA.
DR   EMBL; U09979; AAA18880.1; -; Genomic_DNA.
DR   RefSeq; WP_011969036.1; NC_009617.1.
DR   AlphaFoldDB; P52936; -.
DR   SMR; P52936; -.
DR   STRING; 290402.Cbei_1712; -.
DR   EnsemblBacteria; ABR33884; ABR33884; Cbei_1712.
DR   KEGG; cbe:Cbei_1712; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_072509_0_0_9; -.
DR   OMA; TKELYPM; -.
DR   OrthoDB; 930905at2; -.
DR   Proteomes; UP000000565; Chromosome.
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..273
FT                   /note="Stage 0 sporulation protein A homolog"
FT                   /id="PRO_0000081238"
FT   DOMAIN          7..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        205..224
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   CONFLICT        41
FT                   /note="R -> S (in Ref. 2; AAA18880)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   273 AA;  30684 MW;  DF2E0E5718CD1A48 CRC64;
     MEDSKISVLI ADDNKEFCSI LNDYLLNQKD IVVTGIAKDG REALELIVER KPDLVILDII
     MPHLDGLGVL EKLNTMQLEK VPRIIILSAV GQDKITQQAI TLGADYYTVK PFDMEVFTKR
     IREMFNSSAA VQETNMRNSY ASSMISTPSE NKTKAPIDLE TEITNIIHEV GVPAHIKGYM
     YLREAITMVV NDMELLSAVT KELYPSIAKK YNTTASRVER AIRHAIEVAW GRGQIEAINR
     LFGYTVHNDK GKPTNSEFIA IIADKLRLKN KVS