ID LFTR_ECOK1 Reviewed; 234 AA. AC A1A9C8; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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=Ecok1_07740; ORFNames=APECO1_1204; OS Escherichia coli O1:K1 / APEC. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=405955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17293413; DOI=10.1128/jb.01726-06; RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.; RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 RT shares strong similarities with human extraintestinal pathogenic E. coli RT genomes."; RL J. Bacteriol. 189:3228-3236(2007). 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}. 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; CP000468; ABJ00268.1; -; Genomic_DNA. DR RefSeq; WP_001241673.1; NZ_CADILS010000017.1. DR AlphaFoldDB; A1A9C8; -. DR SMR; A1A9C8; -. DR KEGG; ecv:APECO1_1204; -. DR HOGENOM; CLU_075045_0_0_6; -. DR Proteomes; UP000008216; 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_0000304335" 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 //