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Database: UniProt
Entry: A7VIQ4_9CLOT
LinkDB: A7VIQ4_9CLOT
Original site: A7VIQ4_9CLOT 
ID   A7VIQ4_9CLOT            Unreviewed;       270 AA.
AC   A7VIQ4;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672, ECO:0000256|PIRNR:PIRNR002937};
GN   ORFNames=CLOL250_02813 {ECO:0000313|EMBL:EDO56563.1};
OS   Clostridium sp. L2-50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=411489 {ECO:0000313|EMBL:EDO56563.1, ECO:0000313|Proteomes:UP000003352};
RN   [1] {ECO:0000313|EMBL:EDO56563.1, ECO:0000313|Proteomes:UP000003352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-50 {ECO:0000313|EMBL:EDO56563.1,
RC   ECO:0000313|Proteomes:UP000003352};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium sp. L2-50.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDO56563.1, ECO:0000313|Proteomes:UP000003352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-50 {ECO:0000313|EMBL:EDO56563.1,
RC   ECO:0000313|Proteomes:UP000003352};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Hodges J., Shah N., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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:EDO56563.1}.
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DR   EMBL; AAYW02000020; EDO56563.1; -; Genomic_DNA.
DR   RefSeq; WP_008402921.1; NZ_DS480328.1.
DR   AlphaFoldDB; A7VIQ4; -.
DR   eggNOG; COG2201; Bacteria.
DR   HOGENOM; CLU_072509_0_0_9; -.
DR   OrthoDB; 9793299at2; -.
DR   Proteomes; UP000003352; 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; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR02875; spore_0_A; 1.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR   PANTHER; PTHR48111:SF1; TWO-COMPONENT RESPONSE REGULATOR ORR33; 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|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR002937};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR002937};
KW   Two-component regulatory system {ECO:0000256|PIRNR:PIRNR002937}.
FT   DOMAIN          8..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   270 AA;  30178 MW;  FE25C944BF584A78 CRC64;
     MNNQDISIII ADGDCELVAK QLLANTSRVD IKIVDKVTDG ESAIESIRKY QPDVVLLDIC
     LPVMDGLGVM ETIRDSGDCP ETLFVVITSV GSQRLIRCAF DLGASFYVLK PYNSDQLVAR
     LKQMHERKQE ILAEMSNDLI CIPNKSMTDN VANNIESDVT DIIRDIGIPA NIKGYQYIRE
     GIIMAVNDVN MLNYITKLLY PSIAKKYKTT SSSVERAIRH AIEVAWNRGQ IDVINDIFGY
     TVNAGKGKPT NSEFIALIAD KLRIEYRKRA
//
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