ID   SP0A_CLODI              Reviewed;         274 AA.
AC   P52938;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Stage 0 sporulation protein A homolog;
GN   Name=spo0A;
OS   Clostridioides difficile (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=1496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC   11209 / 90556-M6S;
RA   Putland R.A.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-223.
RC   STRAIN=ATCC 9689 / DSM 1296 / BCRC 10642 / JCM 1296 / NCIMB 10666 / NCTC
RC   11209 / 90556-M6S;
RA   Putland R.A., Grove D.I.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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; U43514; AAB05561.1; -; Genomic_DNA.
DR   EMBL; X94328; CAA63989.1; -; Genomic_DNA.
DR   EMBL; U36481; AAA79509.1; -; Genomic_DNA.
DR   RefSeq; WP_032509222.1; NZ_CP027014.1.
DR   AlphaFoldDB; P52938; -.
DR   SMR; P52938; -.
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..274
FT                   /note="Stage 0 sporulation protein A homolog"
FT                   /id="PRO_0000081240"
FT   DOMAIN          10..128
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         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   274 AA;  30868 MW;  E5B66DCC2EE6F1D0 CRC64;
     MGGFLVEKIK IVLADDNKDF CQVLKEYLSN EDDIDILGIA KDGIEALDLV KKTQPDLLIL
     DVIMPHLDGL GVIEKLNTMD IPKMPKIIVL SAVGQDKITQ SAINLGADYY IVKPFDFVVF
     INRIRELVSN RVTQVEPKPR PVQETQMTRS DFVKNVGNIE TEITNIIHEI GVPAHIKGYL
     YLREAMKMVI DNVELLGAVT KELYPSIAKK FNTTPSRVER AIRHAIEVAW SRGKVDTINQ
     LFGYTVHNTK GKPTNSEFIA MIADKLRLEH SMVK