LFTR_VIBCH
ID LFTR_VIBCH Reviewed; 243 AA.
AC Q9KRA7; O50259;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=VC_1735;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
RX PubMed=9407082; DOI=10.1074/jbc.272.52.33009;
RA Ichetovkin I.E., Abramochkin G., Shrader T.E.;
RT "Substrate recognition by the leucyl/phenylalanyl-tRNA-protein transferase.
RT Conservation within the enzyme family and localization to the trypsin-
RT resistant domain.";
RL J. Biol. Chem. 272:33009-33014(1997).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87633.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94885.1; -; Genomic_DNA.
DR EMBL; AF035002; AAB87633.1; ALT_FRAME; Genomic_DNA.
DR PIR; G82163; G82163.
DR RefSeq; NP_231371.1; NC_002505.1.
DR RefSeq; WP_001029434.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRA7; -.
DR SMR; Q9KRA7; -.
DR STRING; 243277.VC_1735; -.
DR DNASU; 2613740; -.
DR EnsemblBacteria; AAF94885; AAF94885; VC_1735.
DR KEGG; vch:VC_1735; -.
DR PATRIC; fig|243277.26.peg.1658; -.
DR eggNOG; COG2360; Bacteria.
DR HOGENOM; CLU_075045_0_0_6; -.
DR OMA; YRQGIFP; -.
DR BioCyc; VCHO:VC1735-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008914; F:leucyltransferase activity; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT /id="PRO_0000207247"
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
