ID LFTR_XANC3 Reviewed; 249 AA. AC Q8PL03; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 02-SEP-2026, entry version 113. 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=XAC2003; OS Xanthomonas citri pv. citri (strain 306). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Lysobacterales; Lysobacteraceae; Xanthomonas. OX NCBI_TaxID=1203463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(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=N-terminal L-lysyl-[protein] + L-leucyl-tRNA(Leu) = N-terminal CC L-leucyl-L-lysyl-[protein] + tRNA(Leu) + H(+); Xref=Rhea:RHEA:12340, CC Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622, Rhea:RHEA-COMP:12670, CC Rhea:RHEA-COMP:12671, ChEBI:CHEBI:15378, ChEBI:CHEBI:65249, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:133043; EC=2.3.2.6; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00688}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-arginyl-[protein] + L-leucyl-tRNA(Leu) = N- CC terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu) + H(+); 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=L-phenylalanyl-tRNA(Phe) + an N-terminal L-alpha-aminoacyl- CC [protein] = 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; AE008923; AAM36865.1; -; Genomic_DNA. DR RefSeq; WP_011051273.1; NC_003919.1. DR AlphaFoldDB; Q8PL03; -. DR SMR; Q8PL03; -. DR GeneID; 66911139; -. DR KEGG; xac:XAC2003; -. DR eggNOG; COG2360; Bacteria. DR HOGENOM; CLU_075045_0_0_6; -. DR Proteomes; UP000000576; 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 FunFam; 3.30.70.3550:FF:000001; Leucyl/phenylalanyl-tRNA--protein transferase; 1. 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 InterPro; IPR063613; Leu_Phe_trans_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 Pfam; PF30046; Leu_Phe_trans_N; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1..249 FT /note="Leucyl/phenylalanyl-tRNA--protein transferase" FT /id="PRO_0000207250" SQ SEQUENCE 249 AA; 27301 MW; CF7CB2CDE29969B8 CRC64; MARHLPFLLD ADPTAPFPPA AQALRDPDGL LAIGGDLAPQ RLLNAYAHGI FPWFSQDQPI LWWSPDPRMV FRTDALRLSS RFRRQLRSSS WTVRADTAFE QVIDACASVP RAGQDGTWIT AQMQQAYIAL HELGHAHSLE VFDGTRLVGG IYGVAIGQMF FGESMFSAQS GGSKVALAAL AMHLHTEGWP LLDAQVENPH LLSLGAQRLP RAQFLQQVQL QVARPALPGT WSGRYGQRPA SSLGEARLT //