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Database: UniProt
Entry: K4LJ88_9FIRM
LinkDB: K4LJ88_9FIRM
Original site: K4LJ88_9FIRM 
ID   K4LJ88_9FIRM            Unreviewed;       252 AA.
AC   K4LJ88;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=DCF50_p2655 {ECO:0000313|EMBL:AFV06658.1};
OS   Dehalobacter sp. CF.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Dehalobacter.
OX   NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06658.1, ECO:0000313|Proteomes:UP000000482};
RN   [1] {ECO:0000313|EMBL:AFV06658.1, ECO:0000313|Proteomes:UP000000482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AFV06658.1};
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; AFV06658.1; -; Genomic_DNA.
DR   RefSeq; WP_015044685.1; NC_018867.1.
DR   AlphaFoldDB; K4LJ88; -.
DR   STRING; 1131462.DCF50_p2655; -.
DR   KEGG; dec:DCF50_p2655; -.
DR   PATRIC; fig|1131462.4.peg.2682; -.
DR   eggNOG; COG3279; Bacteria.
DR   HOGENOM; CLU_000445_14_1_9; -.
DR   Proteomes; UP000000482; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   CDD; cd17532; REC_LytTR_AlgR-like; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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:SF1; 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:UP000000482}.
FT   DOMAIN          4..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          146..252
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   252 AA;  29125 MW;  5EF5AEF65398787D CRC64;
     MKIRALLVDD ESPARKELRY LLKSFEDVLI VGEAENALEA MELIDSVDYS VIFLDINMPG
     LNGIELARKL SQSPKQPAVI FTTAHEEFAF DAFSVHAYDY LLKPIHPKRL EEALNTVRKR
     KTPAPGQPKT EPVKEDIPEF KPLEVIAAEY NGKTILIRPE EIIYISTDKD NVYVKTEADF
     YLTRYTLRDL ESRLDPKTFF RTHRCYLVNI KKMRELVPYF NGTYTVIVQD KDKSEVPVSR
     TQARRLKEIL GI
//
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