ID F5YL67_TREPZ Unreviewed; 201 AA.
AC F5YL67;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Two component transcriptional regulator, LuxR family {ECO:0000313|EMBL:AEF86356.1};
GN OrderedLocusNames=TREPR_1860 {ECO:0000313|EMBL:AEF86356.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF86356.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF86356.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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DR EMBL; CP001843; AEF86356.1; -; Genomic_DNA.
DR RefSeq; WP_015708279.1; NC_015578.1.
DR AlphaFoldDB; F5YL67; -.
DR STRING; 545694.TREPR_1860; -.
DR KEGG; tpi:TREPR_1860; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_1_12; -.
DR OrthoDB; 359059at2; -.
DR Proteomes; UP000009223; Chromosome.
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 PANTHER; PTHR45566; HTH-TYPE TRANSCRIPTIONAL REGULATOR YHJB-RELATED; 1.
DR PANTHER; PTHR45566:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATOR YHJB-RELATED; 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; PS50043; HTH_LUXR_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:UP000009223}.
FT DOMAIN 3..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 141..201
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 201 AA; 22630 MW; 9BC0171CCE51AFA5 CRC64;
MNTLVLIDDH TMMRRGLASY FTQTGRWQVL GEAGSQEEAL ALFETLSPGP LPGIILLDID
LHGSWGLDLI PRLRNYYEQK PPALIYSVYE DYAHVKAAIR AEAAGYVCKS QGEAELEMAM
DAVLQGRIFF APHLIVKMDA VSDILLCLTK RERQIFGMVQ RSYSNRQIAE ELVVSVRTIE
NNLSIIYDKT GVPGRKELEK L
//
