BPT_BURVG
ID BPT_BURVG Reviewed; 276 AA.
AC A4JE23;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Bcep1808_1519;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000614; ABO54526.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JE23; -.
DR STRING; 269482.Bcep1808_1519; -.
DR EnsemblBacteria; ABO54526; ABO54526; Bcep1808_1519.
DR KEGG; bvi:Bcep1808_1519; -.
DR eggNOG; COG2935; Bacteria.
DR HOGENOM; CLU_077607_0_0_4; -.
DR OMA; MVEDSHV; -.
DR Proteomes; UP000002287; Chromosome 1.
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; Reference proteome; Transferase.
FT CHAIN 1..276
FT /note="Aspartate/glutamate leucyltransferase"
FT /id="PRO_1000045131"
SQ SEQUENCE 276 AA; 31166 MW; EC175FFEF3B750B8 CRC64;
MTHPTELPLS PLSALQFYAT APYPCSYLDG RIARSQVATP SHLINSDIYT ELVKAGFRRS
GVFTYRPYCD GCRACVPVRV PVRAFTPSRT QRRMWKRHRA LVATVSPLHY DEEHYALYMR
YQSARHAGGG MDRDSRDQYE QFLLQSRINS RLVEFRDLDA SGGEPGKLRM VSMIDILGDG
LSSVYTFFEP DDAHTSYGTY NILWQIEQAR SLGLPYVYLG YWIRESPKMA YKANFHPLEG
LLDGRWKTLD PARVDLPPVD AALARAPLPG GHSGAG