ID K4L1C0_9FIRM Unreviewed; 406 AA.
AC K4L1C0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=DCF50_p365 {ECO:0000313|EMBL:AFV04371.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV04371.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV04371.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV04371.1};
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; AFV04371.1; -; Genomic_DNA.
DR RefSeq; WP_015042374.1; NC_018867.1.
DR AlphaFoldDB; K4L1C0; -.
DR STRING; 1131462.DCF50_p365; -.
DR KEGG; dec:DCF50_p365; -.
DR PATRIC; fig|1131462.4.peg.373; -.
DR eggNOG; COG2197; Bacteria.
DR eggNOG; COG4963; Bacteria.
DR HOGENOM; CLU_033160_3_1_9; -.
DR Proteomes; UP000000482; Chromosome.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17535; REC_NarL-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43384:SF17; PARA FAMILY PLASMID PARTITIONING PROTEIN; 1.
DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000482}.
FT DOMAIN 5..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 406 AA; 44621 MW; FF42709E2C7D22FF CRC64;
MQGIRILIVD DIRNTRENIR RILALDSGFE VIGEAGCGSE AIRLAELLKP EIILMDISMP
DIDGIKTTEL LSFRVPNTSI IMMSVENDPD HMTKAMMAGA KSYIVKPFTG KELTSTILNV
YHKESRKREM INSPLSPDSA VKTSDTAAKV ISIFSAKGGV GKTTTAVNLG VELAKSSKVL
LLDLSLQFGD IASFLNLVPK RTITDLVQAG SIKEEDIRLH TLSHSSGLEI LAATNRPEYA
EKVTMEHIGQ ILEEVKIHYD FVILDNTSRF DDISLAGLEA ANEIWVVAGM DIPSIKNTKL
ALEIMHTLDY SPKIKLILNK FEKKIGISMK DIESSLGLNV TYLIPYEEQL TSVLNKGVPF
VEALARSAPA LEIKKMVSTL GVNSEITKKG QDSKETSRLS FLRFGG
//
