ID D4K2T6_9FIRM Unreviewed; 241 AA.
AC D4K2T6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=FP2_01270 {ECO:0000313|EMBL:CBK97829.1};
OS Faecalibacterium prausnitzii L2-6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=718252 {ECO:0000313|EMBL:CBK97829.1, ECO:0000313|Proteomes:UP000008804};
RN [1] {ECO:0000313|EMBL:CBK97829.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK97829.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; FP929045; CBK97829.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K2T6; -.
DR STRING; 718252.FP2_01270; -.
DR KEGG; fpr:FP2_01270; -.
DR PATRIC; fig|718252.3.peg.1904; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_2_9; -.
DR BioCyc; FPRA718252:G1375-102-MONOMER; -.
DR Proteomes; UP000008804; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 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:UP000008804}.
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 131..217
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 241 AA; 28221 MW; 52821569D47D774C CRC64;
MELRFAVVED RLPDAQRLES LLRLAFAGGQ PLVCDHYESG DAFLAAFPSK NYQVVFLDIC
MEGTNGIETA RILRRADPDL LLVFVTSSPE YVWDAFPVHP FDYLLKPYRE EKLFQLADEL
RRVLFRAEPE LEVRIARQQV HLPLRKIQYA MAQNHYVRIV SDDGECRTVS TFSQVEQLLR
AQENFIVCNR GVILNMDKVL RLDSDCFEML DGTRLPVRQK DKNTLFAQFT QYQFRHMRRE
L
//
