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Database: UniProt
Entry: F7K5L1_9FIRM
LinkDB: F7K5L1_9FIRM
Original site: F7K5L1_9FIRM 
ID   F7K5L1_9FIRM            Unreviewed;       432 AA.
AC   F7K5L1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=HMPREF0994_01143 {ECO:0000313|EMBL:EGN42905.1};
OS   Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN42905.1, ECO:0000313|Proteomes:UP000003336};
RN   [1] {ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGN42905.1, ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN42905.1,
RC   ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1.";
RL   Submitted (APR-2013) 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}.
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:EGN42905.1}.
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DR   EMBL; ACTP02000004; EGN42905.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7K5L1; -.
DR   STRING; 658086.HMPREF0994_01143; -.
DR   eggNOG; COG2207; Bacteria.
DR   eggNOG; COG4753; Bacteria.
DR   HOGENOM; CLU_000445_5_0_9; -.
DR   Proteomes; UP000003336; 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; 2.
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:UP000003336}.
FT   DOMAIN          2..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          331..429
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   432 AA;  49231 MW;  A9D721A5BB200A77 CRC64;
     MNVLIVDDQK AIVESLREGI RWEELGVEKV YTACSAREAK LVLVNFPVDV MLSDIEMPEE
     DGLELCQWAK ERLPALECIF LTSHADFSYA REAIRLGSFD YILQPVRYEE VEAVLRKAEG
     KIRENQSVRQ LQNTRKLVVE QRDTILEAIC MKLRQGREGD AEQILSTLKE LLQPDFKKFS
     FYPAVVRIIK WKRIINTWDD KLVRLVIRNV LEELFAAAHG VTCIASMQDG SFVILAAVED
     SLFDEEKWEV GLKEFYDFVE AQMDFSIAVY MGTKLPASEE ESHGPAFGGM LTYLAGVGEE
     LNPSGKSGIF KLADGAGEEA EGNEGEAEPV QKAVSYIKAN LNKNISRTDV AELVHLNEEY
     FSRLFKQQTG ETFKDYILLE KMNMARTLLE RSNLSISIVA SKVGYDNFSH FSKMFKKLTD
     MTPQEYRKEH QK
//
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