LFTR_ECOLI
ID LFTR_ECOLI Reviewed; 234 AA.
AC P0A8P1; P23885;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Leucyl/phenylalanyl-tRNA--protein transferase;
DE EC=2.3.2.6;
DE AltName: Full=L/F-transferase;
DE AltName: Full=Leucyltransferase;
DE AltName: Full=Phenyalanyltransferase;
GN Name=aat; Synonyms=ycaA; OrderedLocusNames=b0885, JW0868;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1909328; DOI=10.1016/s0021-9258(18)55327-8;
RA Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.;
RT "Structure and expression of the infA operon encoding translational
RT initiation factor IF1. Transcriptional control by growth rate.";
RL J. Biol. Chem. 266:16491-16498(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=8331068; DOI=10.1128/jb.175.14.4364-4374.1993;
RA Shrader T.E., Tobias J.W., Varshavsky A.;
RT "The N-end rule in Escherichia coli: cloning and analysis of the leucyl,
RT phenylalanyl-tRNA-protein transferase gene aat.";
RL J. Bacteriol. 175:4364-4374(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 [5]
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 [6]
RP CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=7657641; DOI=10.1074/jbc.270.35.20621;
RA Abramochkin G., Shrader T.E.;
RT "The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and
RT characterization of substrate recognition, domain structure, and secondary
RT structure.";
RL J. Biol. Chem. 270:20621-20628(1995).
CC -!- FUNCTION: Functions in the N-end rule pathway of protein degradation
CC where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-
CC tRNAs to the N-termini of proteins containing an N-terminal arginine or
CC lysine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-
CC terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu);
CC Xref=Rhea:RHEA:12340, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC Rhea:RHEA-COMP:12670, Rhea:RHEA-COMP:12671, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:65249, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC ChEBI:CHEBI:133043; EC=2.3.2.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = H(+) +
CC N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu);
CC Xref=Rhea:RHEA:50416, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC Rhea:RHEA-COMP:12672, Rhea:RHEA-COMP:12673, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64719, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC ChEBI:CHEBI:133044; EC=2.3.2.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-phenylalanyl-
CC tRNA(Phe) = an N-terminal L-phenylalanyl-L-alpha-aminoacyl-[protein]
CC + tRNA(Phe); Xref=Rhea:RHEA:43632, Rhea:RHEA-COMP:9668, Rhea:RHEA-
CC COMP:9699, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10637,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:78597,
CC ChEBI:CHEBI:83561; EC=2.3.2.6;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the L/F-transferase family. {ECO:0000305}.
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; M63145; AAC36910.1; -; Genomic_DNA.
DR EMBL; L10383; AAA03231.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC73971.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35605.1; -; Genomic_DNA.
DR PIR; A36888; A36888.
DR RefSeq; NP_415405.1; NC_000913.3.
DR RefSeq; WP_001241678.1; NZ_STEB01000006.1.
DR PDB; 2CXA; X-ray; 1.60 A; A=1-234.
DR PDB; 2DPS; X-ray; 2.40 A; A/B=1-234.
DR PDB; 2DPT; X-ray; 2.75 A; A/B=1-234.
DR PDB; 2Z3K; X-ray; 2.85 A; A/B=2-234.
DR PDB; 2Z3L; X-ray; 2.75 A; A/B=2-234.
DR PDB; 2Z3M; X-ray; 2.70 A; A/B=2-234.
DR PDB; 2Z3N; X-ray; 2.50 A; A/B=2-234.
DR PDB; 2Z3O; X-ray; 2.40 A; A/B=2-234.
DR PDB; 2Z3P; X-ray; 2.50 A; A/B=2-234.
DR PDBsum; 2CXA; -.
DR PDBsum; 2DPS; -.
DR PDBsum; 2DPT; -.
DR PDBsum; 2Z3K; -.
DR PDBsum; 2Z3L; -.
DR PDBsum; 2Z3M; -.
DR PDBsum; 2Z3N; -.
DR PDBsum; 2Z3O; -.
DR PDBsum; 2Z3P; -.
DR AlphaFoldDB; P0A8P1; -.
DR SMR; P0A8P1; -.
DR BioGRID; 4259988; 43.
DR BioGRID; 849864; 2.
DR DIP; DIP-48235N; -.
DR IntAct; P0A8P1; 10.
DR STRING; 511145.b0885; -.
DR DrugBank; DB08437; Puromycin.
DR jPOST; P0A8P1; -.
DR PaxDb; P0A8P1; -.
DR PRIDE; P0A8P1; -.
DR EnsemblBacteria; AAC73971; AAC73971; b0885.
DR EnsemblBacteria; BAA35605; BAA35605; BAA35605.
DR GeneID; 66670841; -.
DR GeneID; 945490; -.
DR KEGG; ecj:JW0868; -.
DR KEGG; eco:b0885; -.
DR PATRIC; fig|1411691.4.peg.1393; -.
DR EchoBASE; EB1103; -.
DR eggNOG; COG2360; Bacteria.
DR InParanoid; P0A8P1; -.
DR OMA; YRQGIFP; -.
DR PhylomeDB; P0A8P1; -.
DR BioCyc; EcoCyc:EG11112-MON; -.
DR BioCyc; MetaCyc:EG11112-MON; -.
DR BRENDA; 2.3.2.6; 2026.
DR EvolutionaryTrace; P0A8P1; -.
DR PRO; PR:P0A8P1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0016755; F:aminoacyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0008914; F:leucyltransferase activity; IDA:EcoCyc.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.3550; -; 1.
DR Gene3D; 3.40.630.70; -; 1.
DR HAMAP; MF_00688; Leu_Phe_trans; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR004616; Leu/Phe-tRNA_Trfase.
DR InterPro; IPR042203; Leu/Phe-tRNA_Trfase_C.
DR InterPro; IPR042221; Leu/Phe-tRNA_Trfase_N.
DR PANTHER; PTHR30098; PTHR30098; 1.
DR Pfam; PF03588; Leu_Phe_trans; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR00667; aat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..234
FT /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT /id="PRO_0000207217"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2CXA"
FT TURN 21..25
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2Z3P"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2Z3O"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2CXA"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:2CXA"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:2CXA"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2CXA"
SQ SEQUENCE 234 AA; 26619 MW; 8C725890D42ABF6F CRC64;
MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF SPGDPILWWS
PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE GCASDREEGT WITRGVVEAY
HRLHELGHAH SIEVWREDEL VGGMYGVAQG TLFCGESMFS RMENASKTAL LVFCEEFIGH
GGKLIDCQVL NDHTASLGAC EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE
