ID N2APE9_9FIRM Unreviewed; 247 AA.
AC N2APE9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=C823_02101 {ECO:0000313|EMBL:EMZ27960.1};
OS Eubacterium plexicaudatum ASF492.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ27960.1, ECO:0000313|Proteomes:UP000012589};
RN [1] {ECO:0000313|EMBL:EMZ27960.1, ECO:0000313|Proteomes:UP000012589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF492 {ECO:0000313|EMBL:EMZ27960.1,
RC ECO:0000313|Proteomes:UP000012589};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMZ27960.1}.
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DR EMBL; AQFT01000066; EMZ27960.1; -; Genomic_DNA.
DR RefSeq; WP_004061436.1; NZ_AQFT02000001.1.
DR AlphaFoldDB; N2APE9; -.
DR STRING; 1235802.C823_02101; -.
DR GeneID; 78434165; -.
DR PATRIC; fig|1235802.3.peg.2233; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_2_9; -.
DR OrthoDB; 113975at2; -.
DR Proteomes; UP000012589; Unassembled WGS sequence.
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:UP000012589}.
FT DOMAIN 3..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 133..232
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 247 AA; 28969 MW; 0DCFAA614E3501A6 CRC64;
MLKIYVCDDE KEITDLIRTQ IRNYFETYPS EYEVETFNSG SSLINRVNKQ RADIIFLDIE
LSDSNGIQIA KLIRRVDKLV KIVFITNYKN YKGAAFTVRA FGYVEKPSTT EQIFKQLSDI
QKYMREEQND ISIKFETVDG LINLKVKDIL YFESSNRKIS IITFTNEYRM VQKISSLAKL
LEPYDFKSPH SSFLVNLDYV VGIKNYTVYM VNDIEIPLSQ RKVSEFKKAM NHYFMKTIDM
CKGVPHD
//
