ID   TRPR_SALPA              Reviewed;         108 AA.
AC   Q5PK31;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Trp operon repressor {ECO:0000255|HAMAP-Rule:MF_00475};
GN   Name=trpR {ECO:0000255|HAMAP-Rule:MF_00475}; OrderedLocusNames=SPA4393;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(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}.
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DR   EMBL; CP000026; AAV80116.1; -; Genomic_DNA.
DR   RefSeq; WP_000192005.1; NC_006511.1.
DR   AlphaFoldDB; Q5PK31; -.
DR   SMR; Q5PK31; -.
DR   EnsemblBacteria; AAV80116; AAV80116; SPA4393.
DR   KEGG; spt:SPA4393; -.
DR   HOGENOM; CLU_147939_0_0_6; -.
DR   OMA; GQMSQRE; -.
DR   Proteomes; UP000008185; 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   PIRSF; PIRSF003196; 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..108
FT                   /note="Trp operon repressor"
FT                   /id="PRO_0000196501"
FT   DNA_BIND        68..91
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00475"
SQ   SEQUENCE   108 AA;  12392 MW;  A32E5182D48AA30D CRC64;
     MTQHSPYSSA IAEQRNQEWL RFVELLRQAY AEDLHLPLLQ LMLTPDEREA LGTRVRIIEE
     LLRGEMSQRE LKTELGAGIA TITRGSNSLK SAPVELRHWL EQILLKSA