ID   BPT_SPHEL               Reviewed;         260 AA.
AC   P59795;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   25-MAY-2022, entry version 64.
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}; Synonyms=ate1;
OS   Sphingomonas elodea.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=179878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31461 / PS-60;
RX   PubMed=14767675; DOI=10.1007/s10295-004-0118-9;
RA   Harding N.E., Patel Y.N., Coleman R.J.;
RT   "Organization of genes required for gellan polysaccharide biosynthesis in
RT   Sphingomonas elodea ATCC 31461.";
RL   J. Ind. Microbiol. Biotechnol. 31:70-82(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=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; AY220099; AAP46177.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59795; -.
DR   SMR; P59795; -.
DR   STRING; 1081640.AGFU01000034_gene2872; -.
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..260
FT                   /note="Aspartate/glutamate leucyltransferase"
FT                   /id="PRO_0000195116"
SQ   SEQUENCE   260 AA;  28745 MW;  3191C445A2B905A9 CRC64;
     MTALSRFPRF FVTSPSPCPY LPGRQERKIF TELSGQQAGE LNDALSRIGF RRSQSVAYRP
     SCAGCTACVS VRVVTEGFQP NATQRKLLKR YGDLEVTACK PWATGEQYEL LKRYLDSRHP
     GGGMAAMDES DYADMVEQSP VSSYVIEYRE PSVNGERGRL VGACITDQQG DGLSMIYSYF
     VTDDEARPGM GNFIIMDHIL RARAAGLPYV YLGYWVKGSA RMAYKTRYRP IEVLGPTGWA
     LLEDEDMVGA MPSAVAAALA