ID LFTR_PSEPK Reviewed; 226 AA. AC Q88FS7; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 102. 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}; OrderedLocusNames=PP_4005; OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 OS / KT2440). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I., RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.; RT "Complete genome sequence and comparative analysis of the metabolically RT versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). 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; AE015451; AAN69599.1; -; Genomic_DNA. DR RefSeq; NP_746135.1; NC_002947.4. DR RefSeq; WP_003251213.1; NC_002947.4. DR AlphaFoldDB; Q88FS7; -. DR SMR; Q88FS7; -. DR STRING; 160488.PP_4005; -. DR PaxDb; 160488-PP_4005; -. DR GeneID; 83679292; -. DR KEGG; ppu:PP_4005; -. DR PATRIC; fig|160488.4.peg.4261; -. DR eggNOG; COG2360; Bacteria. DR HOGENOM; CLU_075045_0_0_6; -. DR OrthoDB; 9790282at2; -. DR PhylomeDB; Q88FS7; -. DR BioCyc; PPUT160488:G1G01-4272-MONOMER; -. DR Proteomes; UP000000556; 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..226 FT /note="Leucyl/phenylalanyl-tRNA--protein transferase" FT /id="PRO_0000207235" SQ SEQUENCE 226 AA; 25194 MW; 260CB53304D496D7 CRC64; MLTWLTRDSL TFPPLEKALH DPNGLLAAGG DLSPERLVQA YRHGCFPWYQ DGQPILWWSP DPRTVLLPDQ LHVSRSLAKL MRQGRYQVSF DTDFPAVIAA CAAPRDYADG TWITDTMRNA YCELHRRGIA HSVEVRQDGE LVGGLYGLAM GQLFFGESMF SRADNASKVG FVTLVNHLRD AGFVLIDCQM PTNHLHSLGA HAISRAEFAS YLARHLDQPN SASWVA //