ID A5I124_CLOBH Unreviewed; 239 AA.
AC A5I124; A7G2T1;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=CBO1186 {ECO:0000313|EMBL:CAL82735.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82735.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82735.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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}.
CC -!- FUNCTION: Required for high-level post-exponential phase expression of
CC a series of secreted proteins. {ECO:0000256|ARBA:ARBA00037164}.
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DR EMBL; AM412317; CAL82735.1; -; Genomic_DNA.
DR RefSeq; WP_011948826.1; NC_009698.1.
DR RefSeq; YP_001253711.1; NC_009495.1.
DR RefSeq; YP_001387096.1; NC_009698.1.
DR AlphaFoldDB; A5I124; -.
DR GeneID; 5185441; -.
DR KEGG; cbh:CLC_1229; -.
DR KEGG; cbo:CBO1186; -.
DR PATRIC; fig|413999.7.peg.1174; -.
DR HOGENOM; CLU_000445_14_6_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR046947; LytR-like.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR37299:SF3; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR PANTHER; PTHR37299; TRANSCRIPTIONAL REGULATOR-RELATED; 1.
DR Pfam; PF04397; LytTR; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00850; LytTR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 3..126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 141..239
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 239 AA; 28553 MW; 71BA2C45C06629B7 CRC64;
MLRVMICEDN EVHRVKLKQI VENTILREKL DLDIVLATEN PQEIISYIKE NRSTGIYLLD
VDLKNDINGI KLGEKIRELD PLGYIIFTTT HLEMSYLAFK YKVEAMDYVI KDDDDFKERV
NSCIIKAYNR YHKQEHEEEY ISIDTDTRII NIRPSDILFI ETTGTPHKIR IHEENRQIEM
YANLKDIQKK LPSNFYRCHK SYIVNKNKIE EIDKNHNKII MKNEEECYVS FRYMRGLIV
//
