ID   BPT_HELHP               Reviewed;         241 AA.
AC   P59794;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
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}; OrderedLocusNames=HH_1829;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP78426.1; -; Genomic_DNA.
DR   RefSeq; WP_011116668.1; NC_004917.1.
DR   AlphaFoldDB; P59794; -.
DR   SMR; P59794; -.
DR   STRING; 235279.HH_1829; -.
DR   EnsemblBacteria; AAP78426; AAP78426; HH_1829.
DR   KEGG; hhe:HH_1829; -.
DR   eggNOG; COG2935; Bacteria.
DR   HOGENOM; CLU_077607_0_0_7; -.
DR   OMA; MVEDSHV; -.
DR   OrthoDB; 1675133at2; -.
DR   Proteomes; UP000002495; Chromosome.
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..241
FT                   /note="Aspartate/glutamate leucyltransferase"
FT                   /id="PRO_0000195104"
SQ   SEQUENCE   241 AA;  28906 MW;  BED0EC274348B66C CRC64;
     MRLVEFYSEK KVCSYIDSKQ SIFRYFHIQN VTPSFYYGLL ERGWRRFGNY FFTPMCEGCT
     DCISIRTLID DFTFSRNHKR LLKKAQNIDI YIQKPTITQA HIELYNRYHR VMRDKKGWEY
     TPTTPESYMD MFVEGHQDFG YEILYFIDSQ LVGVGLVDAL FDSITAVYFY YDHTFAHHSL
     GTLNILKQIQ IGKENGLKYF YPGYWIKDHY CMGYKQRFTP FEVLKNIPDV FEAPIWEMYN
     G