ID   BPT_RHILO               Reviewed;         254 AA.
AC   Q983E4;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 106.
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};
GN   Name=bpt {ECO:0000255|HAMAP-Rule:MF_00689, ECO:0000303|PubMed:16492767};
GN   OrderedLocusNames=mll8364;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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};
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, ECO:0000305}.
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DR   EMBL; BA000012; BAB53937.1; -; Genomic_DNA.
DR   RefSeq; WP_010915563.1; NC_002678.2.
DR   AlphaFoldDB; Q983E4; -.
DR   STRING; 266835.14027668; -.
DR   EnsemblBacteria; BAB53937; BAB53937; BAB53937.
DR   GeneID; 66684602; -.
DR   KEGG; mlo:mll8364; -.
DR   eggNOG; COG2935; Bacteria.
DR   HOGENOM; CLU_077607_1_0_5; -.
DR   OMA; MVEDSHV; -.
DR   OrthoDB; 1675133at2; -.
DR   Proteomes; UP000000552; 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   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..254
FT                   /note="Aspartate/glutamate leucyltransferase"
FT                   /id="PRO_0000195112"
SQ   SEQUENCE   254 AA;  29100 MW;  A94E2AADC905F876 CRC64;
     MTQHPTQSPQ FFLTAPSPCP YLDGQFERKV FTHLVGDKAS EMNDLLTQGG FRRSQNIAYR
     PACETCRACV SVRILAQEFT ASRNMKRVLQ HNSDLVGAMH NAEPSTEQYS LFRSYLDARH
     RRGGMSDMTV LDYAMMVEDT HVDTKVIEYR RRGPDTFITG KGQGELIAVA LTDKMADGLS
     MVYSYFNPEF EERSLGTFMI LDHIARARAM GLPHVYLGYW VNGSRKMNYK MRFMPQEHLG
     PKGWERYTNE AVSR