ID   SP0A_CLOPA              Reviewed;         273 AA.
AC   P52940;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Stage 0 sporulation protein A homolog;
GN   Name=spo0A;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
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}.
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; U09982; AAA18883.1; -; Unassigned_DNA.
DR   PIR; S60880; S60880.
DR   AlphaFoldDB; P52940; -.
DR   SMR; P52940; -.
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_0000081242"
FT   DOMAIN          7..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        201..220
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"
SQ   SEQUENCE   273 AA;  30601 MW;  686E32B0D66411E3 CRC64;
     MEYSKISVLI ADDNKEFCNI LNDYLLNQSD IVVVGIAKDG IEALKLIEEK KPDLVILDII
     MPNMDGLVVL EKLANINIDP VPNVIVLSAV GQDKITQRAI TLGADYYVVK PFDMDVFTKR
     IRQMFNNTIL DSETKKTMPI SEKAADVKIS QSVPLDLEDE SIIHEIGVPA HIKGYMYLRE
     AINMVVDNIE LLSAVTKELY PSIAKKYNTT ASRVERAIRH AIEVAWSRGQ VDTINKLFGY
     TIHNGKGKPT NSEFIAMIAD KLRLKNKVKN VAQ