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TRPR_SHIF8
ID   TRPR_SHIF8              Reviewed;         108 AA.
AC   Q0SX19;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Trp operon repressor {ECO:0000255|HAMAP-Rule:MF_00475};
GN   Name=trpR {ECO:0000255|HAMAP-Rule:MF_00475}; OrderedLocusNames=SFV_4427;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF06396.1; -; Genomic_DNA.
DR   RefSeq; WP_000068679.1; NC_008258.1.
DR   AlphaFoldDB; Q0SX19; -.
DR   SMR; Q0SX19; -.
DR   EnsemblBacteria; ABF06396; ABF06396; SFV_4427.
DR   GeneID; 66671719; -.
DR   KEGG; sfv:SFV_4427; -.
DR   HOGENOM; CLU_147939_0_0_6; -.
DR   OMA; GQMSQRE; -.
DR   BioCyc; SFLE373384:SFV_RS24355-MON; -.
DR   Proteomes; UP000000659; 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_1000014050"
FT   DNA_BIND        68..91
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00475"
SQ   SEQUENCE   108 AA;  12355 MW;  FDFF8A60EC4FE7BE CRC64;
     MAQQSPYSAA MAEQRHQEWL RFVDLLKNAY QNDLHLPLLN LMLTPDEREA LGTRVRIVEE
     LLRGEMSQRE LKNELGAGIA TITRGSNSLK AAPVELRQWL EEVLLKSD
 
 
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