ID LFTR_SALTI Reviewed; 234 AA. AC P67614; Q8XEV8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 04-NOV-2026, entry version 115. 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=STY0953, t1979; OS Salmonella typhi. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., RA Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella enterica RT serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., RA Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and RT CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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; AL513382; CAD05355.1; -; Genomic_DNA. DR EMBL; AE014613; AAO69592.1; -; Genomic_DNA. DR RefSeq; WP_001241650.1; NZ_CALNVT020000001.1. DR SMR; P67614; -. DR STRING; 220341.gene:17584946; -. DR KEGG; stt:t1979; -. DR KEGG; sty:STY0953; -. DR PATRIC; fig|220341.7.peg.961; -. DR eggNOG; COG2360; Bacteria. DR HOGENOM; CLU_075045_0_0_6; -. DR OMA; AAESMFH; -. DR FunFam; 3.30.70.3550:FF:000001; Leucyl/phenylalanyl-tRNA--protein transferase; 1. DR FunFam; 3.40.630.70: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; IPR063612; Leu_Phe_trans_C. DR InterPro; IPR063613; Leu_Phe_trans_N. 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. DR NCBIfam; TIGR00667; aat; 1. 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 Proteomes; UP000002670; Chromosome. DR AlphaFoldDB; P67614; -. 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_0000207241" SQ SEQUENCE 234 AA; 26673 MW; E6EBFFA7F9B8D5B5 CRC64; MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQHGIFPWF SPGDPILWWS PDPRAVLWPE KFHLSRSMKR FHNASPYRVT LNYAFDRVID GCANHRDEGT WITRGIEEAY RRLHELGHAH SIEVWRDREL VGGMYGVSQG ALFCGESMFS RQENASKTAL LVFCAEFTRH GGKLIDCQVL NSHTASLGAI EIPRRDYLDH LAALRQQPLA SRFWVPRTLF LPRK //