ID E3PS89_ACESD Unreviewed; 289 AA.
AC E3PS89;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=CLOST_1623 {ECO:0000313|EMBL:CBH21743.1};
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH21743.1, ECO:0000313|Proteomes:UP000007041};
RN [1] {ECO:0000313|Proteomes:UP000007041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000313|Proteomes:UP000007041};
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
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; FP565809; CBH21743.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PS89; -.
DR STRING; 1511.CLOST_1623; -.
DR KEGG; cst:CLOST_1623; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_959540_0_0_9; -.
DR BioCyc; CSTI499177:GJE9-1677-MONOMER; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17906; CheX; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.1550.10; CheC-like; 1.
DR InterPro; IPR028976; CheC-like_sf.
DR InterPro; IPR028051; CheX-like_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43228; TWO-COMPONENT RESPONSE REGULATOR; 1.
DR PANTHER; PTHR43228:SF1; TWO-COMPONENT RESPONSE REGULATOR ARR22; 1.
DR Pfam; PF13690; CheX; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF103039; CheC-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000007041}.
FT DOMAIN 5..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 289 AA; 31825 MW; 4C07B6D8B5517A7D CRC64;
MSKLKAMIVD DSSFSITILK SLLEKKGFEI VCEAQSIAEI KDEILDCKPD LVTMDMTLSD
GDGIEATKLI LNHSPNAKVM AISAMMDAEI IKQAKDAGAR AYIQKPIDED EFNSAIDKLF
AGEELYRLLS ENYFGAFREA LISYLKKLEA APLVHNEEQI NENIKSKKSS GISVTIGIIG
RHCGRLVIDM SDDTIIELAK RALNKSELAK DEMIAFFGEF GNIVGGNACS MLNTFNRGLS
LRVSPPTIFH GKDLTISIGE IKSTSLVLQS NAGEIFMNIG FQRGDDEWM
//