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Database: UniProt
Entry: N2A3N6_9FIRM
LinkDB: N2A3N6_9FIRM
Original site: N2A3N6_9FIRM 
ID   N2A3N6_9FIRM            Unreviewed;       222 AA.
AC   N2A3N6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=C823_04817 {ECO:0000313|EMBL:EMZ20700.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ20700.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ20700.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ20700.1,
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:EMZ20700.1}.
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DR   EMBL; AQFT01000140; EMZ20700.1; -; Genomic_DNA.
DR   AlphaFoldDB; N2A3N6; -.
DR   STRING; 1235802.C823_04817; -.
DR   PATRIC; fig|1235802.3.peg.5072; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_4_9; -.
DR   OrthoDB; 1655504at2; -.
DR   Proteomes; UP000012589; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd17574; REC_OmpR; 1.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.690; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR   PANTHER; PTHR48111:SF2; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012589};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          125..222
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        125..222
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   222 AA;  25669 MW;  CF24E46CE77E26DB CRC64;
     MKKIAIIEDD TDICNMITKF LINHNYEVYS APNGREGIDL CQKFLPDLII LDLMLPILNG
     DSVIKQLRTY TDIPVIVVSA KTMVQSKIDL LRLGADDYMT KPFNLFELLA RIEANLKRSV
     TAPMKADIHL KYKDIKIENC NAYIKGAIVQ FTSTELSILI LLLQYPQKIF SKQNIYESIW
     QEEYAYDNDT INTHISNIRK KIKKHTDTDY IETVWGIGYK LK
//
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