ID A0A1G4WCG1_9FIRM Unreviewed; 243 AA.
AC A0A1G4WCG1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02910339_02845 {ECO:0000313|EMBL:SCX20301.1};
OS Lachnospiraceae bacterium YSD2013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX20301.1, ECO:0000313|Proteomes:UP000199278};
RN [1] {ECO:0000313|EMBL:SCX20301.1, ECO:0000313|Proteomes:UP000199278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSD2013 {ECO:0000313|EMBL:SCX20301.1,
RC ECO:0000313|Proteomes:UP000199278};
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; FMTX01000035; SCX20301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4WCG1; -.
DR STRING; 1520828.SAMN02910339_02845; -.
DR OrthoDB; 1769137at2; -.
DR Proteomes; UP000199278; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR42713; HISTIDINE KINASE-RELATED; 1.
DR PANTHER; PTHR42713:SF3; TRANSCRIPTIONAL REGULATORY PROTEIN HPTR; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF00072; Response_reg; 1.
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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000199278}.
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 142..240
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 243 AA; 27722 MW; 6D1A9FAE195D1906 CRC64;
MYRVMLIDDE QSARSLLKAS INWERYDMEV AGEAASGIEA INIIDEIVPD IAFVDISMPF
MNGIEFTEVA TKRYPGLKII IMTAFDEFEY ARQCIRLPVF DYMLKPFVRS EVEENLKKLK
DILDSTVKDA EPAVEIEPSS IGQIKRYIED NYTDSKLNLT SVAQIFGFSA SYLSRKFKQD
TGKNFVEYLT ECRMKRAMEL AAGNMKMFSA SNEVGIPDPN YFGRCFKKYT GQSYSDYASS
VSK
//
