ID   BPT_VIBVU               Reviewed;         232 AA.
AC   Q8DAR7;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Aspartate/glutamate leucyltransferase {ECO:0000255|HAMAP-Rule:MF_00689, ECO:0000305};
DE            EC=2.3.2.29 {ECO:0000255|HAMAP-Rule:MF_00689, ECO:0000269|PubMed:16492767};
DE   AltName: Full=Bacterial protein transferase {ECO:0000303|PubMed:16492767};
GN   Name=bpt {ECO:0000255|HAMAP-Rule:MF_00689, ECO:0000303|PubMed:16492767};
GN   OrderedLocusNames=VV1_2124;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION.
RA   Rhee J.H., Kim S.Y., Chung S.S., Lee S.E., Choy H.E.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-18; TYR-58; TYR-170
RP   AND TYR-205.
RX   PubMed=16492767; DOI=10.1073/pnas.0511224103;
RA   Graciet E., Hu R.G., Piatkov K., Rhee J.H., Schwarz E.M., Varshavsky A.;
RT   "Aminoacyl-transferases and the N-end rule pathway of
RT   prokaryotic/eukaryotic specificity in a human pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3078-3083(2006).
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, ECO:0000269|PubMed:16492767}.
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, ECO:0000269|PubMed:16492767};
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, ECO:0000269|PubMed:16492767};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00689,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the R-transferase family. Bpt subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00689, ECO:0000305}.
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DR   EMBL; AE016795; AAO10511.2; -; Genomic_DNA.
DR   RefSeq; WP_011080005.1; NC_004459.3.
DR   AlphaFoldDB; Q8DAR7; -.
DR   SMR; Q8DAR7; -.
DR   EnsemblBacteria; AAO10511; AAO10511; VV1_2124.
DR   KEGG; vvu:VV1_2124; -.
DR   HOGENOM; CLU_077607_0_0_6; -.
DR   OMA; MVEDSHV; -.
DR   BioCyc; MetaCyc:MON-19912; -.
DR   Proteomes; UP000002275; 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   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..232
FT                   /note="Aspartate/glutamate leucyltransferase"
FT                   /id="PRO_0000207256"
FT   MUTAGEN         18
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16492767"
FT   MUTAGEN         58
FT                   /note="Y->F: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:16492767"
FT   MUTAGEN         170
FT                   /note="Y->F: Almost loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16492767"
FT   MUTAGEN         205
FT                   /note="Y->F: Almost loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16492767"
SQ   SEQUENCE   232 AA;  27378 MW;  C60EA1E9550116D3 CRC64;
     MSSDIHQIKI GLTDNHPCSY LPERKERVAV ALEADMHTAD NYEVLLANGF RRSGNTIYKP
     HCDSCHSCQP IRISVPDIEL SRSQKRLLAK ARSLSWSMKR NMDENWFDLY SRYIVARHRN
     GTMYPPKKDD FAHFSRNQWL TTQFLHIYEG QRLIAVAVTD IMDHCASAFY TFFEPEHELS
     LGTLAVLFQL EFCQEEKKQW LYLGYQIDEC PAMNYKVRFH RHQKLVNQRW QG