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Database: UniProt
Entry: R6Q7D6_9FIRM
LinkDB: R6Q7D6_9FIRM
Original site: R6Q7D6_9FIRM 
ID   R6Q7D6_9FIRM            Unreviewed;       258 AA.
AC   R6Q7D6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672, ECO:0000256|PIRNR:PIRNR002937};
GN   ORFNames=BN563_00719 {ECO:0000313|EMBL:CDC32613.1};
OS   Eubacterium sp. CAG:251.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262886 {ECO:0000313|EMBL:CDC32613.1, ECO:0000313|Proteomes:UP000018414};
RN   [1] {ECO:0000313|EMBL:CDC32613.1, ECO:0000313|Proteomes:UP000018414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:251 {ECO:0000313|Proteomes:UP000018414};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDC32613.1}.
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DR   EMBL; CBFD010000027; CDC32613.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6Q7D6; -.
DR   STRING; 1262886.BN563_00719; -.
DR   Proteomes; UP000018414; 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   CDD; cd00156; REC; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000018414};
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          6..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   258 AA;  29449 MW;  85DEEE8FBC6BFC0E CRC64;
     MEKKLKVLIA DNSNQFATQC QKELETQGYE VSTMENDGAK VFDAIAKQKF DVILMDVFMT
     NEDAVDVLEY YQTHTVEKPI IAVLSTISSE ELEKQTMSLG ADYFFIKPIL PAQVAKRITR
     LTAWKNEHKA EIQKGRAMFE QDMDVVISDI MRQIGVPAHI KGYHYLRTAI KYCLDDSEML
     SSVTKILYPS VAKKYKTTSS RVERAIRHAI EVAWDRGDVD VLSSYFGYTI QSERGKPTNS
     EFIAMITDKI NLSMRNSM
//
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