ID F3AI59_9FIRM Unreviewed; 266 AA.
AC F3AI59;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672, ECO:0000256|PIRNR:PIRNR002937};
GN ORFNames=HMPREF0987_00133 {ECO:0000313|EMBL:EGG90258.1};
OS Lachnospiraceae bacterium 9_1_43BFAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658088 {ECO:0000313|EMBL:EGG90258.1, ECO:0000313|Proteomes:UP000003620};
RN [1] {ECO:0000313|EMBL:EGG90258.1, ECO:0000313|Proteomes:UP000003620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_1_43BFAA {ECO:0000313|EMBL:EGG90258.1,
RC ECO:0000313|Proteomes:UP000003620};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 9_1_43BFAA.";
RL Submitted (MAR-2011) 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:EGG90258.1}.
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DR EMBL; ACTX01000001; EGG90258.1; -; Genomic_DNA.
DR AlphaFoldDB; F3AI59; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_072509_0_0_9; -.
DR Proteomes; UP000003620; 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:SF14; SPORULATION INITIATION PHOSPHOTRANSFERASE F; 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:UP000003620};
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 5..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
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 266 AA; 30356 MW; F444AC199BD858A3 CRC64;
MGKLNVAIAD DNERMLDLLG ELIDRDKELT LVGKANNGED MCKIIEQKQP DVVLLDLIMP
KMDGLSVMEQ INTDKKIKKH PSFIVVTAVG QEQMTEDAFE KGANYYIMKP FNNRMLLDKI
KHVNRVYRPA APDRELESSR KDLPEYDLEE EVTDMIHEIG IPAHIKGYHY LRDAIIMAVE
DMDVLNAITK ILYPTVAKKN QTTSSRVERA IRHAIEVAWT RGKLETIDEM FGYTVSSGKG
KPTNSEFIAL LADTIRLRGR RRQLVE
//
