ID LFTR_CHRVO Reviewed; 233 AA. AC Q7NX31; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 112. 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=CV_1798; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC OS 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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=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; AE016825; AAQ59472.1; -; Genomic_DNA. DR RefSeq; WP_011135350.1; NC_005085.1. DR AlphaFoldDB; Q7NX31; -. DR SMR; Q7NX31; -. DR STRING; 243365.CV_1798; -. DR KEGG; cvi:CV_1798; -. DR eggNOG; COG2360; Bacteria. DR HOGENOM; CLU_075045_0_0_4; -. DR OrthoDB; 9790282at2; -. DR Proteomes; UP000001424; 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..233 FT /note="Leucyl/phenylalanyl-tRNA--protein transferase" FT /id="PRO_0000207213" SQ SEQUENCE 233 AA; 26447 MW; 83E71C266E753148 CRC64; MIPWLGPEPV FPPVSQALSH PNGLLAAGGD LSSRRILTAY SEGIFPWFSD GEPILWWSPA PRMVMFPDEL KVSRSLAKTL RNLDYEIRVD SAFPEVMRAC AEPRAGQDGT WIVPEMVAAY CRLHQIGYAH SFETWIDGEL AGGLYGVSIG RMFYGESMFS RRRDASKLAF VHMVRHLQAQ GVTMIDCQMH TEHLASLGAR LISRDVFLAT LKENVRHPQP DRMWDYHYRH ESS //