ID   LFTR_XYLFM              Reviewed;         244 AA.
AC   B0U6R3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=Xfasm12_0789;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA11779.1; -; Genomic_DNA.
DR   RefSeq; WP_004083748.1; NC_010513.1.
DR   AlphaFoldDB; B0U6R3; -.
DR   SMR; B0U6R3; -.
DR   KEGG; xfm:Xfasm12_0789; -.
DR   HOGENOM; CLU_075045_0_0_6; -.
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; Transferase.
FT   CHAIN           1..244
FT                   /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT                   /id="PRO_1000131959"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   244 AA;  27528 MW;  122BA5D3526EFAE4 CRC64;
     MHSQPYLLSP APNNTPFPPA EHALREPNGL LAIGGDLTPQ RLLAAYRSGI FPWFTEGQPP
     LWWSPDPRTV FHSDSIHLSR RFRRSLRTST WRVRADTMFA AVIDACASTP RRGQDGTWIT
     ANMREAYLTL HQHGYAHSVE VFDGTMLVGG IYGVAIGRMF FGESMFSTHN GASKIALASL
     AYFLHTHSVP LIDAQVENQH LLNLGAERWP RRDFLTYVRR LITQTELPAC WSVLFGEKLS
     RDLV
//