BPT_METC4
ID BPT_METC4 Reviewed; 248 AA.
AC B7KPZ2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Mchl_4611;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) 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; CP001298; ACK85385.1; -; Genomic_DNA.
DR RefSeq; WP_003606575.1; NC_011757.1.
DR AlphaFoldDB; B7KPZ2; -.
DR EnsemblBacteria; ACK85385; ACK85385; Mchl_4611.
DR KEGG; mch:Mchl_4611; -.
DR HOGENOM; CLU_077607_1_0_5; -.
DR OMA; MVEDSHV; -.
DR BioCyc; MEXT440085:MCHL_RS22460-MON; -.
DR Proteomes; UP000002385; 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; Transferase.
FT CHAIN 1..248
FT /note="Aspartate/glutamate leucyltransferase"
FT /id="PRO_1000147805"
SQ SEQUENCE 248 AA; 28162 MW; 0150A4FCB7FC418A CRC64;
MTSHPRDTPQ FYLTAPSPCP YLPGQEERKV FTHLVGRRAR DLNEILTQGG FRRSQTIAYR
PACETCRACV SVRVVVEDFA ITGSQRRILQ RNAELIGTPE PNRPASEQYA LFRRYLDARH
GDGGMVDMTV LDYAMMIEDS HVDTHLVVYR ERGPDSAIHG RGVGAPVAVC LTDVLADGLS
MVYSFYDPDE ASRSLGTYMI LDHIRRARAL GLPYLYLGYW VDGSRKMDYK AKFKPQERLM
PQGWVRVE