BPT_ACIAC
ID BPT_ACIAC Reviewed; 245 AA.
AC A1TRT1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Aave_3105;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-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; CP000512; ABM33669.1; -; Genomic_DNA.
DR RefSeq; WP_011796179.1; NC_008752.1.
DR AlphaFoldDB; A1TRT1; -.
DR SMR; A1TRT1; -.
DR STRING; 397945.Aave_3105; -.
DR EnsemblBacteria; ABM33669; ABM33669; Aave_3105.
DR KEGG; aav:Aave_3105; -.
DR eggNOG; COG2935; Bacteria.
DR HOGENOM; CLU_077607_0_0_4; -.
DR OMA; MVEDSHV; -.
DR OrthoDB; 1675133at2; -.
DR Proteomes; UP000002596; 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..245
FT /note="Aspartate/glutamate leucyltransferase"
FT /id="PRO_1000045119"
SQ SEQUENCE 245 AA; 28453 MW; A63D06E547B7F913 CRC64;
MTQLNDLPLQ TLQFYATAPY PCSYLPDRQA RSQVATPSHL IQSDVYSDLV ARGFRRSGMF
TYRPYCDGCQ ACTPLRVLAG EFRPDRSQRR AWKQHSILQT RVLRLCYEPE HYQLYLHYQR
ARHSGGGMDH DSIDQYTQFL LQSRVNSRLV EFRDPAPDGE TGTLRMVSIL DVLDDGLSAV
YTFYDPDPDC SYGTFNVLWQ IEQARTLGLA HVYLGYWIAE SAKMNYKSRF HPHELRVHGE
WQRGT