LPTN_ECOLI
ID LPTN_ECOLI Reviewed; 24 AA.
AC P0AD89; P09408; Q2M820;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Tryptophanase operon leader peptide;
GN Name=tnaC; Synonyms=tnaL; OrderedLocusNames=b3707, JW3685;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3902796; DOI=10.1128/jb.164.2.731-740.1985;
RA Stewart V., Yanofsky C.;
RT "Evidence for transcription antitermination control of tryptophanase operon
RT expression in Escherichia coli K-12.";
RL J. Bacteriol. 164:731-740(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=12228716; DOI=10.1126/science.1073997;
RA Gong F., Yanofsky C.;
RT "Instruction of translating ribosome by nascent peptide.";
RL Science 297:1864-1867(2002).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 5-24 IN TNAC-STALLED
RP 50S RIBOSOMAL SUBUNIT.
RC STRAIN=K12 / A19 / KC6;
RX PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA Bischoff L., Berninghausen O., Beckmann R.;
RT "Molecular basis for the ribosome functioning as an L-tryptophan sensor.";
RL Cell Rep. 9:469-475(2014).
CC -!- FUNCTION: Required for tryptophan-regulated expression of the tna
CC operon. In the presence of free L-Trp release of this nascent peptide
CC by release factor 2 is inhibited and the ribosome stalls with the last
CC amino acid in the P site and a UGA stop codon in the A site. This
CC prevent transcripiton termination factor Rho binding, and thus allows
CC transcription and translation of TnaA and TnaB.
CC {ECO:0000269|PubMed:12228716}.
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DR EMBL; M11990; AAA24678.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62058.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76730.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77586.1; -; Genomic_DNA.
DR PIR; I54862; I54862.
DR RefSeq; NP_418163.1; NC_000913.3.
DR RefSeq; WP_001364348.1; NZ_STEB01000015.1.
DR PDB; 4UY8; EM; 3.80 A; 7=5-24.
DR PDB; 5M6S; EM; 4.80 A; A=2-24.
DR PDB; 6I0Y; EM; 3.20 A; 7=1-24.
DR PDBsum; 4UY8; -.
DR PDBsum; 5M6S; -.
DR PDBsum; 6I0Y; -.
DR AlphaFoldDB; P0AD89; -.
DR SMR; P0AD89; -.
DR BioGRID; 4262592; 20.
DR STRING; 511145.b3707; -.
DR PaxDb; P0AD89; -.
DR PRIDE; P0AD89; -.
DR EnsemblBacteria; AAC76730; AAC76730; b3707.
DR EnsemblBacteria; BAE77586; BAE77586; BAE77586.
DR GeneID; 66672393; -.
DR GeneID; 948223; -.
DR KEGG; ecj:JW3685; -.
DR KEGG; eco:b3707; -.
DR EchoBASE; EB1254; -.
DR HOGENOM; CLU_221068_0_0_6; -.
DR BioCyc; EcoCyc:EG11276-MON; -.
DR PRO; PR:P0AD89; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0090358; P:positive regulation of tryptophan metabolic process; IMP:EcoCyc.
DR GO; GO:0031556; P:transcriptional attenuation by ribosome; IDA:EcoCyc.
DR InterPro; IPR012620; Trp_operon_leader_peptide.
DR Pfam; PF08053; Tna_leader; 1.
DR TIGRFAMs; TIGR02616; tnaC_leader; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Leader peptide; Reference proteome.
FT PEPTIDE 1..24
FT /note="Tryptophanase operon leader peptide"
FT /id="PRO_0000044011"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:6I0Y"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:6I0Y"
SQ SEQUENCE 24 AA; 2894 MW; 66E3987EA7C052F9 CRC64;
MNILHICVTS KWFNIDNKIV DHRP
