ID A0A1I0QPJ8_9FIRM Unreviewed; 219 AA.
AC A0A1I0QPJ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN05216413_1904 {ECO:0000313|EMBL:SEW29367.1};
OS Ruminococcaceae bacterium KH2T8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1855400 {ECO:0000313|EMBL:SEW29367.1, ECO:0000313|Proteomes:UP000198503};
RN [1] {ECO:0000313|EMBL:SEW29367.1, ECO:0000313|Proteomes:UP000198503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2T8 {ECO:0000313|EMBL:SEW29367.1,
RC ECO:0000313|Proteomes:UP000198503};
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; FOIY01000004; SEW29367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QPJ8; -.
DR STRING; 1855400.SAMN05216413_1904; -.
DR OrthoDB; 9779069at2; -.
DR Proteomes; UP000198503; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; cd06170; LuxR_C_like; 1.
DR CDD; cd17535; REC_NarL-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR039420; WalR-like.
DR PANTHER; PTHR43214; TWO-COMPONENT RESPONSE REGULATOR; 1.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000198503};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 3..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 156..219
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 219 AA; 24122 MW; 9196BA2ADAA7826D CRC64;
MAKIFMVDDE PLLMESLEII LTYSGGHYIC GFSFNGVDAL EKLDKKTPDQ LPDVMLVDLN
MPQMGGIELI RKVKAKYPDI KIIVLTTFYD EKNISQALAG GAIGYLLKDS GKDAIINAVD
RALQGQSVLD GKVMEKITHM MAGASSEGTK KSDNTDIFEG KDLTDREKEI CRLIAEGCTN
SQIASILFIS EGTVKNYISS IYDKFDVHDR AKLALMLKG
//
