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Database: UniProt
Entry: A0A1H7RI76_9FIRM
LinkDB: A0A1H7RI76_9FIRM
Original site: A0A1H7RI76_9FIRM 
ID   A0A1H7RI76_9FIRM        Unreviewed;       244 AA.
AC   A0A1H7RI76;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=SAMN04487770_11334 {ECO:0000313|EMBL:SEL59544.1};
OS   Butyrivibrio sp. ob235.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1761780 {ECO:0000313|EMBL:SEL59544.1, ECO:0000313|Proteomes:UP000199418};
RN   [1] {ECO:0000313|EMBL:SEL59544.1, ECO:0000313|Proteomes:UP000199418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB235 {ECO:0000313|EMBL:SEL59544.1,
RC   ECO:0000313|Proteomes:UP000199418};
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; FOBE01000013; SEL59544.1; -; Genomic_DNA.
DR   RefSeq; WP_026498715.1; NZ_FOBE01000013.1.
DR   AlphaFoldDB; A0A1H7RI76; -.
DR   OrthoDB; 1974963at2; -.
DR   Proteomes; UP000199418; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd17536; REC_YesN-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   PANTHER; PTHR43280; ARAC-FAMILY TRANSCRIPTIONAL REGULATOR; 1.
DR   PANTHER; PTHR43280:SF2; BIFUNCTIONAL TRANSCRIPTIONAL ACTIVATOR_DNA REPAIR ENZYME ADAA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199418}.
FT   DOMAIN          2..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          146..244
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   244 AA;  28239 MW;  158B2BFBB960B9DC CRC64;
     MNLLIIDDEY YIVQGLVGMI NKEELGFDHI FTAYSAQQGM TILKKEQVDL MLLDIEMPKE
     TGLELLEQLN VEGLQPTTII LSGHQRFDYA QEAMHYHCFN YLLKPIGKQN LNQELSRAMA
     FLRPKQVNPE SEAGNGIKIN DSSFVHTVRR YIRDHLSDAD LNRVKIADAI HLNPDYLSFC
     FHKEFETTLT AYINSKRMDQ AKYLLKNTTM SISDIAEQVG IPNTSYFYRQ FKKTTGQTPQ
     QYRK
//
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