ID   TRPR_YERPS              Reviewed;         125 AA.
AC   Q66EU5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Trp operon repressor {ECO:0000255|HAMAP-Rule:MF_00475};
GN   Name=trpR {ECO:0000255|HAMAP-Rule:MF_00475}; OrderedLocusNames=YPTB0596;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: This protein is an aporepressor. When complexed with L-
CC       tryptophan it binds the operator region of the trp operon (5'-
CC       ACTAGT-'3') and prevents the initiation of transcription. The complex
CC       also regulates trp repressor biosynthesis by binding to its regulatory
CC       region. {ECO:0000255|HAMAP-Rule:MF_00475}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00475}.
CC   -!- SIMILARITY: Belongs to the TrpR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00475}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX936398; CAH19836.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q66EU5; -.
DR   SMR; Q66EU5; -.
DR   EnsemblBacteria; CAH19836; CAH19836; YPTB0596.
DR   KEGG; yps:YPTB0596; -.
DR   OMA; GQMSQRE; -.
DR   Proteomes; UP000001011; Chromosome.
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:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1270.10; -; 1.
DR   HAMAP; MF_00475; Trp_repressor; 1.
DR   InterPro; IPR000831; Trp_repress.
DR   InterPro; IPR013335; Trp_repress_bac.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   InterPro; IPR038116; TrpR-like_sf.
DR   PANTHER; PTHR38025; PTHR38025; 1.
DR   Pfam; PF01371; Trp_repressor; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   TIGRFAMs; TIGR01321; TrpR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..125
FT                   /note="Trp operon repressor"
FT                   /id="PRO_0000196506"
FT   DNA_BIND        84..107
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00475"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   125 AA;  13818 MW;  30A2B09EAEA29B88 CRC64;
     MTDEKQVSDS LNRQTAGNPY SAADPALSAE DNQHWLSFVA LLQNAITQDL HLPLLQLMLT
     PDERTALGTR VRIIEELMRG ELSQRELKSQ LGAGIATITR GSNSLKTAPP QLKSWLEAQL
     LANKR