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Database: UniProt
Entry: N2AI95_9FIRM
LinkDB: N2AI95_9FIRM
Original site: N2AI95_9FIRM 
ID   N2AI95_9FIRM            Unreviewed;       257 AA.
AC   N2AI95;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=C823_02568 {ECO:0000313|EMBL:EMZ26213.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ26213.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ26213.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ26213.1,
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:EMZ26213.1}.
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DR   EMBL; AQFT01000082; EMZ26213.1; -; Genomic_DNA.
DR   AlphaFoldDB; N2AI95; -.
DR   STRING; 1235802.C823_02568; -.
DR   PATRIC; fig|1235802.3.peg.2716; -.
DR   eggNOG; COG3279; Bacteria.
DR   HOGENOM; CLU_000445_14_2_9; -.
DR   OrthoDB; 9774865at2; -.
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          20..132
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          160..211
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         69
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   257 AA;  29684 MW;  4C06AC6B94D7D6A6 CRC64;
     MENFIGWTDA NAQSIRDAIC VAICDDEAFM LELLEEKIKN MLPSAVIEQF SSGRELLEGN
     TQADILFLDI QMPEMDGMET ARLFRRQQKD TLIIFITAAP EYVFQAFDVG AFHYLVKPLS
     DDKFDEVFGN ALLGIRRRNK GRDGDDGDYM MIQAGGVHTK ILFKDIIYAE VFNRKVIIHT
     INGDTEYYGK LSDLEKKAGE DFFRPHRSYL IHFKYVLRYD AVSAVMENGT ALIAKQNYPK
     FVKQYLKYNQ RKGREIR
//
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