TRPR_PECCP
ID TRPR_PECCP Reviewed; 115 AA.
AC C6DF27;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Trp operon repressor {ECO:0000255|HAMAP-Rule:MF_00475};
GN Name=trpR {ECO:0000255|HAMAP-Rule:MF_00475}; OrderedLocusNames=PC1_3676;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT14691.1; -; Genomic_DNA.
DR RefSeq; WP_015841805.1; NC_012917.1.
DR AlphaFoldDB; C6DF27; -.
DR SMR; C6DF27; -.
DR STRING; 561230.PC1_3676; -.
DR EnsemblBacteria; ACT14691; ACT14691; PC1_3676.
DR KEGG; pct:PC1_3676; -.
DR eggNOG; COG2973; Bacteria.
DR HOGENOM; CLU_147939_0_0_6; -.
DR OMA; GQMSQRE; -.
DR OrthoDB; 1926997at2; -.
DR Proteomes; UP000002736; 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..115
FT /note="Trp operon repressor"
FT /id="PRO_1000206375"
FT DNA_BIND 68..91
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00475"
SQ SEQUENCE 115 AA; 12627 MW; 6BD0FE93BD6168E0 CRC64;
MTPLSLLDPA LSEQDNEHWL RFVALLQQSI AEDLQLPLLQ LLLTPDERTA LGTRVRIVQE
LMRGEMSQRE LKSELGAGIA TITRGSNSLK AAPPALKSWL EAQLLSADKP LGDDA