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Database: UniProt
Entry: C0B746_9FIRM
LinkDB: C0B746_9FIRM
Original site: C0B746_9FIRM 
ID   C0B746_9FIRM            Unreviewed;       237 AA.
AC   C0B746;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672, ECO:0000256|PIRNR:PIRNR002937};
GN   ORFNames=COPCOM_00967 {ECO:0000313|EMBL:EEG90739.1};
OS   Coprococcus comes ATCC 27758.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=470146 {ECO:0000313|EMBL:EEG90739.1, ECO:0000313|Proteomes:UP000003793};
RN   [1] {ECO:0000313|EMBL:EEG90739.1, ECO:0000313|Proteomes:UP000003793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27758 {ECO:0000313|EMBL:EEG90739.1,
RC   ECO:0000313|Proteomes:UP000003793};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG90739.1, ECO:0000313|Proteomes:UP000003793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27758 {ECO:0000313|EMBL:EEG90739.1,
RC   ECO:0000313|Proteomes:UP000003793};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Coprococcus comes (ATCC 27758).";
RL   Submitted (MAR-2009) 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.
CC       {ECO:0000256|ARBA:ARBA00024867, ECO:0000256|PIRNR:PIRNR002937}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002937,
CC         ECO:0000256|PIRSR:PIRSR002937-1};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR002937,
CC       ECO:0000256|PIRSR:PIRSR002937-1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR002937}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEG90739.1}.
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DR   EMBL; ABVR01000037; EEG90739.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0B746; -.
DR   HOGENOM; CLU_072509_0_0_9; -.
DR   Proteomes; UP000003793; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   NCBIfam; TIGR02875; spore_0_A; 1.
DR   PANTHER; PTHR44591:SF3; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
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; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR002937};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR002937};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR002937};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002937};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR002937,
KW   ECO:0000256|PIRSR:PIRSR002937-1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR002937};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969, ECO:0000256|PIRNR:PIRNR002937};
KW   Transcription {ECO:0000256|PIRNR:PIRNR002937};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR002937};
KW   Two-component regulatory system {ECO:0000256|PIRNR:PIRNR002937}.
FT   DOMAIN          1..100
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT   MOD_RES         32
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   237 AA;  26924 MW;  91400DDBC384BC88 CRC64;
     MIKISNWWEK ARNGEDIYHI IRDKQPDVVL LDLIMPKMDG ISVMEMIGAD KTVKKQPNFI
     IVTAIGQERI TEDAFEKGAA YYILKPFRNE TILQRIKSSG HAEKSVAPYT DYTVYAEPSE
     EDLETQVTEL LHEIGIPAHI KGYHYLRDSI LMAVDDMEVL NAITKILYPT VAKKNQTTSS
     RVERAIRHAI EVAWSRGKLD TLEALFGYTV SNGKGKPTNS EFIALVADTI RLKSKRR
//
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