ID   LFTR_BRUA2              Reviewed;         204 AA.
AC   Q2YNP4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 78.
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=BAB1_0923;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ10879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM040264; CAJ10879.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2YNP4; -.
DR   SMR; Q2YNP4; -.
DR   STRING; 359391.BAB1_0923; -.
DR   EnsemblBacteria; CAJ10879; CAJ10879; BAB1_0923.
DR   KEGG; bmf:BAB1_0923; -.
DR   HOGENOM; CLU_075045_1_1_5; -.
DR   PhylomeDB; Q2YNP4; -.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008914; F:leucyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.3550; -; 1.
DR   Gene3D; 3.40.630.70; -; 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   PANTHER; PTHR30098; PTHR30098; 1.
DR   Pfam; PF03588; Leu_Phe_trans; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR00667; aat; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..204
FT                   /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT                   /id="PRO_0000258047"
SQ   SEQUENCE   204 AA;  23153 MW;  ED8CE300226856E9 CRC64;
     MTAEAPPDDD IIEPEMLLRA YATGIFPMAE EADDPEVFWV RPEKRGVIPL DGFHIPRSLQ
     KTIRQGIFKI RLDSNFAGVI EGCASGTGER ARTWINEPIR RAYAKLFEIG HCHTVEAWYE
     GKLAGGLYGV TLGRAFFGES MFTRKRDASK VCLAYLVQHL SRQGFVLLDT QFTTPHLERF
     GALEVPRKEY EEMLERALEG IARF