ID   BPT_ACIAD               Reviewed;         271 AA.
AC   Q6FDS2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   10-JUN-2026, entry version 122.
DE   RecName: Full=Aspartate/glutamate leucyltransferase {ECO:0000255|HAMAP-Rule:MF_00689};
DE            EC=2.3.2.29 {ECO:0000255|HAMAP-Rule:MF_00689};
GN   Name=bpt {ECO:0000255|HAMAP-Rule:MF_00689};
GN   OrderedLocusNames=ACIAD0888;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Functions in the N-end rule pathway of protein degradation
CC       where it conjugates Leu from its aminoacyl-tRNA to the N-termini of
CC       proteins containing an N-terminal aspartate or glutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_00689}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-glutamyl-[protein] + L-leucyl-tRNA(Leu) = N-
CC         terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu) + H(+);
CC         Xref=Rhea:RHEA:50412, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC         Rhea:RHEA-COMP:12664, Rhea:RHEA-COMP:12668, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64721, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC         ChEBI:CHEBI:133041; EC=2.3.2.29; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00689};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-aspartyl-[protein] + L-leucyl-tRNA(Leu) = N-
CC         terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu) + H(+);
CC         Xref=Rhea:RHEA:50420, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC         Rhea:RHEA-COMP:12669, Rhea:RHEA-COMP:12674, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64720, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC         ChEBI:CHEBI:133042; EC=2.3.2.29; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00689};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00689}.
CC   -!- SIMILARITY: Belongs to the R-transferase family. Bpt subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00689}.
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DR   EMBL; CR543861; CAG67786.1; -; Genomic_DNA.
DR   RefSeq; WP_004922110.1; NC_005966.1.
DR   AlphaFoldDB; Q6FDS2; -.
DR   SMR; Q6FDS2; -.
DR   STRING; 202950.GCA_001485005_02636; -.
DR   GeneID; 45233348; -.
DR   KEGG; aci:ACIAD0888; -.
DR   eggNOG; COG2935; Bacteria.
DR   HOGENOM; CLU_077607_0_0_6; -.
DR   OrthoDB; 9782022at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04100-MONOMER; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004057; F:arginyl-tRNA--protein transferase activity; IEA:InterPro.
DR   GO; GO:0008914; F:leucyl-tRNA--protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:InterPro.
DR   HAMAP; MF_00689; Bpt; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR017138; Asp_Glu_LeuTrfase.
DR   InterPro; IPR030700; N-end_Aminoacyl_Trfase.
DR   InterPro; IPR007472; N-end_Aminoacyl_Trfase_C.
DR   InterPro; IPR007471; N-end_Aminoacyl_Trfase_N.
DR   NCBIfam; NF002341; PRK01305.1-1; 1.
DR   NCBIfam; NF002342; PRK01305.1-3; 1.
DR   NCBIfam; NF002346; PRK01305.2-3; 1.
DR   PANTHER; PTHR21367; ARGININE-TRNA-PROTEIN TRANSFERASE 1; 1.
DR   PANTHER; PTHR21367:SF1; ARGINYL-TRNA--PROTEIN TRANSFERASE 1; 1.
DR   Pfam; PF04377; ATE_C; 1.
DR   Pfam; PF04376; ATE_N; 1.
DR   PIRSF; PIRSF037208; ATE_pro_prd; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..271
FT                   /note="Aspartate/glutamate leucyltransferase"
FT                   /id="PRO_0000195093"
SQ   SEQUENCE   271 AA;  31991 MW;  03ED19B2D5E873FC CRC64;
     MKSYQPKSLL NDLQYYITPP HDCSYLDNKS ARMVFLDPIH RIDVVTLSEL SRVGFRRSGD
     FVYRPECHLC RQCLSCRVPV HDFNMNSLQK KAWKRNQDLR MSIVPTHAAT SVHYQLYERY
     INERHADGDM FPPSLDQFEK FLVHSCTESF FLELWKDDRL ICVSTCDLMD DGLSAVYTFF
     DPDENRRSLG VFAILKQLEY VKSIDLDYLY LGYWVPHSQK MNYKSQYIPL ELLLDGQWRR
     LNRALSQEEI SQLGESLMTI LPSEWNSMII K
//