BPT_MARMM
ID BPT_MARMM Reviewed; 254 AA.
AC Q0APD6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=Mmar10_1559;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) 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; CP000449; ABI65851.1; -; Genomic_DNA.
DR RefSeq; WP_011643498.1; NC_008347.1.
DR AlphaFoldDB; Q0APD6; -.
DR SMR; Q0APD6; -.
DR STRING; 394221.Mmar10_1559; -.
DR EnsemblBacteria; ABI65851; ABI65851; Mmar10_1559.
DR KEGG; mmr:Mmar10_1559; -.
DR eggNOG; COG2935; Bacteria.
DR HOGENOM; CLU_077607_1_0_5; -.
DR OMA; MVEDSHV; -.
DR OrthoDB; 1675133at2; -.
DR Proteomes; UP000001964; 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..254
FT /note="Aspartate/glutamate leucyltransferase"
FT /id="PRO_0000263191"
SQ SEQUENCE 254 AA; 29097 MW; 9EA837C5C78DA5FA CRC64;
MTHPFATKQI PFFLTASAPC PYLPGRFERK VFTRIDIGEG PALNDALTHA GFRRSQGVLY
RPACEACDAC KSVRIDAEAF EWKRRWRKIA ARNRDLHVSI DAQTATMEQF DLLSRYLDSR
HGDGDMAGMS FGEYVMMVEE GAQRTHVTEY RDSDGVLRAA ALTDVLKDGL SLIYSYFDPE
WERRSPGAYM ILDAVRQAEL AGLPFVYLGY WVRQSRKMSY KAQYQPLQVL TPSGWQPHAE
LAYHDMEDEE DDFD