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Database: UniProt
Entry: A0A1G6DX79_9FIRM
LinkDB: A0A1G6DX79_9FIRM
Original site: A0A1G6DX79_9FIRM 
ID   A0A1G6DX79_9FIRM        Unreviewed;       119 AA.
AC   A0A1G6DX79;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=SAMN02910317_02533 {ECO:0000313|EMBL:SDB49720.1};
OS   Ruminococcaceae bacterium FB2012.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB49720.1, ECO:0000313|Proteomes:UP000199364};
RN   [1] {ECO:0000313|EMBL:SDB49720.1, ECO:0000313|Proteomes:UP000199364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB2012 {ECO:0000313|EMBL:SDB49720.1,
RC   ECO:0000313|Proteomes:UP000199364};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMXS01000015; SDB49720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6DX79; -.
DR   STRING; 1520817.SAMN02910317_02533; -.
DR   OrthoDB; 9790669at2; -.
DR   Proteomes; UP000199364; Unassembled WGS sequence.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR44591:SF14; SPORULATION INITIATION PHOSPHOTRANSFERASE F; 1.
DR   PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199364}.
FT   DOMAIN          3..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   119 AA;  12379 MW;  D95AA7DA84F2BF5D CRC64;
     MSRILFTDDD PMMLRMAGFI MKKTGNEALT ASSGEEGLAK LKSESPDMVF IDIEMPGMSG
     LEMLAQIKQD SSIASVPVCL MSGTVTDGIK AQAAELGALG VIGKPLQAAE VTSVIASAL
//
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