ID Q97JP0_CLOAB Unreviewed; 300 AA.
AC Q97JP0;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN Name=chev {ECO:0000313|EMBL:AAK79205.1};
GN OrderedLocusNames=CA_C1233 {ECO:0000313|EMBL:AAK79205.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79205.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK79205.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79205.1; -; Genomic_DNA.
DR PIR; B97052; B97052.
DR RefSeq; NP_347865.1; NC_003030.1.
DR RefSeq; WP_010964546.1; NC_003030.1.
DR AlphaFoldDB; Q97JP0; -.
DR STRING; 272562.CA_C1233; -.
DR GeneID; 44997740; -.
DR KEGG; cac:CA_C1233; -.
DR PATRIC; fig|272562.8.peg.1433; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0835; Bacteria.
DR HOGENOM; CLU_048995_0_1_9; -.
DR OMA; RLEWNQV; -.
DR OrthoDB; 9806105at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR024181; Chemotax_regulator_CheV.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR47233; CHEMOTAXIS PROTEIN CHEV; 1.
DR PANTHER; PTHR47233:SF3; CHEMOTAXIS PROTEIN CHEV; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002867; CheV; 1.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT DOMAIN 13..151
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 172..299
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 232
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 300 AA; 33406 MW; B646B7FA11C6841B CRC64;
MESNILLESG TGELEILEFV IGDRHFAINI IKVKEVVEVD GGKITKLPET NPAIAGLILC
RNEIITLVDL KYVVNKGAKV ESCSKVIICE FNKVRVAFNI DAIIGVHRVK WEEILKPDDV
SENSLVIAHV LLGQKILLML DFEKIVTDIS PSTGISQERI GNIEYKDRSN IKIAMADDST
LIRKLIKDTL TKAGFTKLEL FDDGKQLLDY LEAISKEKGD RVTDEVQLVI TDIEMPQMDG
HALTRKIKEN PLLRKLPVII FSSLITSELK HKGESVGANA QISKPEVGEL VRIIDELVSK
//