ID   LFTR_XANCB              Reviewed;         249 AA.
AC   B0RT37;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 86.
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=xcc-b100_2268;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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}.
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DR   EMBL; AM920689; CAP51623.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RT37; -.
DR   SMR; B0RT37; -.
DR   KEGG; xca:xcc-b100_2268; -.
DR   HOGENOM; CLU_075045_0_0_6; -.
DR   Proteomes; UP000001188; 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_1000131957"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  27335 MW;  F15725F5E534C693 CRC64;
     MSRTLPHLLS PDPASPFPPA ERALREPDGL LAIGGDLHPQ RLLNAYAHGI FPWFSDGQPL
     LWWSPNPRTV FRTDAIHLSS RFRRQLRTCT WTLRADTAFA QVIAACASSP RPGQDGTWIT
     DQMQEAYLDL HRRGYAHSVE VFDGARLVGG IYGVAIGQMF FGESMFSGAS GGSKIALAAL
     AAKLHGLGWP LIDAQVENAH LMRLGAQRLP REQFLQHVAT QVALPEPPGS WTQRYGERHA
     SGLAGVRLT
//