ID   LFTR_ECO45              Reviewed;         234 AA.
AC   B7MHJ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Leucyl/phenylalanyl-tRNA--protein transferase {ECO:0000255|HAMAP-Rule:MF_00688};
DE            EC=2.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00688};
DE   AltName: Full=L/F-transferase {ECO:0000255|HAMAP-Rule:MF_00688};
DE   AltName: Full=Leucyltransferase {ECO:0000255|HAMAP-Rule:MF_00688};
DE   AltName: Full=Phenyalanyltransferase {ECO:0000255|HAMAP-Rule:MF_00688};
GN   Name=aat {ECO:0000255|HAMAP-Rule:MF_00688};
GN   OrderedLocusNames=ECS88_0914;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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. {ECO:0000255|HAMAP-Rule:MF_00688}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00688};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00688};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00688};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00688}.
CC   -!- SIMILARITY: Belongs to the L/F-transferase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00688}.
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DR   EMBL; CU928161; CAR02248.1; -; Genomic_DNA.
DR   RefSeq; WP_001241673.1; NC_011742.1.
DR   AlphaFoldDB; B7MHJ7; -.
DR   SMR; B7MHJ7; -.
DR   KEGG; ecz:ECS88_0914; -.
DR   HOGENOM; CLU_075045_0_0_6; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008914; F:leucyl-tRNA--protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.630.70; Leucyl/phenylalanyl-tRNA-protein transferase, C-terminal domain; 1.
DR   Gene3D; 3.30.70.3550; Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain; 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   NCBIfam; TIGR00667; aat; 1.
DR   PANTHER; PTHR30098; LEUCYL/PHENYLALANYL-TRNA--PROTEIN TRANSFERASE; 1.
DR   PANTHER; PTHR30098:SF2; LEUCYL_PHENYLALANYL-TRNA--PROTEIN TRANSFERASE; 1.
DR   Pfam; PF03588; Leu_Phe_trans; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..234
FT                   /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT                   /id="PRO_1000131918"
SQ   SEQUENCE   234 AA;  26704 MW;  79724D84D52ABE74 CRC64;
     MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF SPGDPILWWS
     PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE GCASDREEGT WITRGVVEAY
     HRLHELGHAH SIEVWREDEL VGGMYGVAQG TLFCGESMFS RMENASKTAL LVFCDEFIRH
     GGKLIDCQVL NDHTASLGAC EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE
//