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Database: UniProt
Entry: N2B176_9FIRM
LinkDB: N2B176_9FIRM
Original site: N2B176_9FIRM 
ID   N2B176_9FIRM            Unreviewed;       234 AA.
AC   N2B176;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=C823_01005 {ECO:0000313|EMBL:EMZ35312.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ35312.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ35312.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ35312.1,
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:EMZ35312.1}.
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DR   EMBL; AQFT01000029; EMZ35312.1; -; Genomic_DNA.
DR   AlphaFoldDB; N2B176; -.
DR   STRING; 1235802.C823_01005; -.
DR   PATRIC; fig|1235802.3.peg.1079; -.
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..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          131..229
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   234 AA;  27602 MW;  8B1C34EEA1245585 CRC64;
     MIRIAICDDE KHMSDHIRSM VSDFFGKKNQ EISLRMFSSG EELLSYNAQI DILFLDIQMK
     EMDGMETARK LRADQFRGFL VFITVLKEMV FQSFEVQAYD YLVKPVDKKQ FEKTMERLCA
     SMQNASEDSL LVQKRYEGRI IPKDEIVFCE IIDRKIYLNL ASGEVVDYYE RIENLETKLD
     KRFYRCHRSY LINLKHLKGY KNGTACMDNG KEIPVSRLRS KEFSGVVLQY MKNI
//
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