ID C1FPM3_CLOBJ Unreviewed; 221 AA.
AC C1FPM3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=CLM_2186 {ECO:0000313|EMBL:ACO87070.1};
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO87070.1, ECO:0000313|Proteomes:UP000001374};
RN [1] {ECO:0000313|EMBL:ACO87070.1, ECO:0000313|Proteomes:UP000001374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001581; ACO87070.1; -; Genomic_DNA.
DR RefSeq; WP_012705671.1; NC_012563.1.
DR AlphaFoldDB; C1FPM3; -.
DR KEGG; cby:CLM_2186; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_9; -.
DR Proteomes; UP000001374; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17574; REC_OmpR; 1.
DR CDD; cd00383; trans_reg_C; 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; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR PANTHER; PTHR48111:SF32; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 127..221
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 127..221
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 221 AA; 25621 MW; 785E37AACEA67A18 CRC64;
MPKRILVVED DFDIHTIISE VLKESGYLVE VATDGLIAVE MFRRGNFDLI ILDVMLPKID
GFVVCEIIRK ESSVPIIMLT ALGEEEDEMK GFELKVDDYI TKPFSINLLI KRVEAVLRRA
NGLEENNSTL TFEEITIYPS NYKTLVNNKE IELTYKEFQI LEILMSNVGR VFSRESLLNQ
IWGYDYFGDT RVIDTHIKNL RQKLNIDYIK TIRGVGYKIE K
//
