ID   BPT_BURM9               Reviewed;         276 AA.
AC   A2S373;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=BMA10229_A0393;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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=L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) +
CC         N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu);
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=L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) +
CC         N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu);
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; CP000546; ABN02175.1; -; Genomic_DNA.
DR   RefSeq; WP_004192823.1; NC_008836.1.
DR   AlphaFoldDB; A2S373; -.
DR   EnsemblBacteria; ABN02175; ABN02175; BMA10229_A0393.
DR   GeneID; 56595657; -.
DR   KEGG; bml:BMA10229_A0393; -.
DR   HOGENOM; CLU_077607_0_0_4; -.
DR   OMA; MVEDSHV; -.
DR   Proteomes; UP000002283; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004057; F:arginyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008914; F:leucyltransferase activity; IEA:InterPro.
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   PANTHER; PTHR21367; PTHR21367; 2.
DR   Pfam; PF04377; ATE_C; 1.
DR   Pfam; PF04376; ATE_N; 1.
DR   PIRSF; PIRSF037208; ATE_pro_prd; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..276
FT                   /note="Aspartate/glutamate leucyltransferase"
FT                   /id="PRO_1000045127"
SQ   SEQUENCE   276 AA;  31209 MW;  A453F2CA29198D6A CRC64;
     MTHPTELPLS PLSALQFYAT APYPCSYLDG RVARSQVATP SHLINSDIYT ELVKAGFRRS
     GVFTYRPYCD GCRACVPVRV PVDAFAPNRT QRRTWKRHRA LVATVAALHY DEEHYALYMR
     YQSARHAGGG MDRDSRDQYE QFLLQSRINS RLVEFRDLDP AENGASTLRM VSMIDILGDG
     LSSVYTFFDP DESHASYGTY NILWQIEQAK SLRLPYVYLG YWIRESPKMA YKANFHPLEG
     LVDGRWKVLD PTLADLPPVD AALARAPLPG GHSGTR