ID   LFTR_NITEU              Reviewed;         236 AA.
AC   Q82ST5;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   04-NOV-2026, entry version 106.
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=NE2219;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(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; AL954747; CAD86131.1; -; Genomic_DNA.
DR   RefSeq; WP_011112712.1; NC_004757.1.
DR   AlphaFoldDB; Q82ST5; -.
DR   SMR; Q82ST5; -.
DR   STRING; 228410.NE2219; -.
DR   GeneID; 309186168; -.
DR   KEGG; neu:NE2219; -.
DR   eggNOG; COG2360; Bacteria.
DR   HOGENOM; CLU_075045_0_0_4; -.
DR   OMA; AAESMFH; -.
DR   OrthoDB; 9790282at2; -.
DR   PhylomeDB; Q82ST5; -.
DR   Proteomes; UP000001416; 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   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   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..236
FT                   /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT                   /id="PRO_0000207231"
SQ   SEQUENCE   236 AA;  26753 MW;  4B9B02337539B397 CRC64;
     MIRTLYSDTP FPPLEQALIE PNGLLAAGGD LSPERLISAY RQGIFPWFNP GEIILWWSPD
     PRMVLFPREL KISRSLHKTL KKNDYQIRTD SAFTEVMQAC AAPREDQAGT WIHEEMIAAY
     TALHQMGVAH SVETWIEGEL AGGLYGVAIG RAFFGESMFS RATDASKIAL VHLARQLENW
     GYGLIDCQMK TAHLMSMGAR EIPRSQFSKR LNQLNALPGQ NRKWYFDFTY PGRSEQ
//