LFTR_VIBCM
ID LFTR_VIBCM Reviewed; 243 AA.
AC C3LN57;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Leucyl/phenylalanyl-tRNA--protein transferase {ECO:0000255|HAMAP-Rule:MF_00688};
DE EC=2.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00688};
DE AltName: Full=L/F-transferase {ECO:0000255|HAMAP-Rule:MF_00688};
DE AltName: Full=Leucyltransferase {ECO:0000255|HAMAP-Rule:MF_00688};
DE AltName: Full=Phenyalanyltransferase {ECO:0000255|HAMAP-Rule:MF_00688};
GN Name=aat {ECO:0000255|HAMAP-Rule:MF_00688}; OrderedLocusNames=VCM66_1675;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- FUNCTION: Functions in the N-end rule pathway of protein degradation
CC where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-
CC tRNAs to the N-termini of proteins containing an N-terminal arginine or
CC lysine. {ECO:0000255|HAMAP-Rule:MF_00688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-
CC terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu);
CC Xref=Rhea:RHEA:12340, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC Rhea:RHEA-COMP:12670, Rhea:RHEA-COMP:12671, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:65249, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC ChEBI:CHEBI:133043; EC=2.3.2.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = H(+) +
CC N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu);
CC Xref=Rhea:RHEA:50416, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC Rhea:RHEA-COMP:12672, Rhea:RHEA-COMP:12673, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64719, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC ChEBI:CHEBI:133044; EC=2.3.2.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-phenylalanyl-
CC tRNA(Phe) = an N-terminal L-phenylalanyl-L-alpha-aminoacyl-[protein]
CC + tRNA(Phe); Xref=Rhea:RHEA:43632, Rhea:RHEA-COMP:9668, Rhea:RHEA-
CC COMP:9699, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10637,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:78597,
CC ChEBI:CHEBI:83561; EC=2.3.2.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00688};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00688}.
CC -!- SIMILARITY: Belongs to the L/F-transferase family. {ECO:0000255|HAMAP-
CC Rule:MF_00688}.
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DR EMBL; CP001233; ACP05983.1; -; Genomic_DNA.
DR RefSeq; WP_001029434.1; NC_012578.1.
DR AlphaFoldDB; C3LN57; -.
DR SMR; C3LN57; -.
DR EnsemblBacteria; ACP05983; ACP05983; VCM66_1675.
DR KEGG; vcm:VCM66_1675; -.
DR HOGENOM; CLU_075045_0_0_6; -.
DR OMA; YRQGIFP; -.
DR Proteomes; UP000001217; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008914; F:leucyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.3550; -; 1.
DR Gene3D; 3.40.630.70; -; 1.
DR HAMAP; MF_00688; Leu_Phe_trans; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR004616; Leu/Phe-tRNA_Trfase.
DR InterPro; IPR042203; Leu/Phe-tRNA_Trfase_C.
DR InterPro; IPR042221; Leu/Phe-tRNA_Trfase_N.
DR PANTHER; PTHR30098; PTHR30098; 1.
DR Pfam; PF03588; Leu_Phe_trans; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR00667; aat; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..243
FT /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT /id="PRO_1000147797"
SQ SEQUENCE 243 AA; 27569 MW; 24AF885AE888D515 CRC64;
MAIYLTELSP ETLTFPSPFT ALDDPNGLLA FGGDLRLERI WAAYQQGIFP WYGPEDPILW
WSPSPRAVFD PTRFQPAKSV KKFQRKHQYR VSVNHATSQV IEQCALTRPA DQRWLNDSMR
HAYGELAKQG RCHSVEVWQG EQLVGGLYGI SVGQLFCGES MFSLATNASK IALWYFCDHF
SRHQGQLIDC QVMNPHLQSL GATTLSREQF IQSLLSFKEK QVLSGCFETQ WLATPTSPCA
FED
