ID K4L6A7_9FIRM Unreviewed; 231 AA.
AC K4L6A7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN Name=phoP {ECO:0000313|EMBL:AFV06807.1};
GN ORFNames=DCF50_p2804 {ECO:0000313|EMBL:AFV06807.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06807.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV06807.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV06807.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
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; CP003870; AFV06807.1; -; Genomic_DNA.
DR RefSeq; WP_015044836.1; NC_018867.1.
DR AlphaFoldDB; K4L6A7; -.
DR STRING; 1131462.DCF50_p2804; -.
DR KEGG; dec:DCF50_p2804; -.
DR PATRIC; fig|1131462.4.peg.2833; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_1_9; -.
DR Proteomes; UP000000482; 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; cd00383; trans_reg_C; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.690; -; 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; IPR016032; Sig_transdc_resp-reg_C-effctor.
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:SF40; SENSORY TRANSDUCTION PROTEIN REGX3; 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; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000482};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 4..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 130..229
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 130..229
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 231 AA; 26378 MW; A04DDC58E67276B0 CRC64;
MSKRILVVED EEAIARLISY NLQKEGFEVQ VSGDGLEALG KIRSEKPDLL ILDIMLPGMD
GYEICQAVRK EDSSLPVIML SARDDELDKI LGLELGGDDY LTKPFSPREL IARVRALLRR
AQTTQAAPDH ETFLIDRLAV DFSGREISVN DQIVPLTPKE FELLEYLIRH RGKVVSRDQL
LDRVWNYDFA GDTRIVDVHI SRLREKIEPD PKNPSYIQTV RGVGYRFKER G
//
