LFTR_LEPIC
ID LFTR_LEPIC Reviewed; 219 AA.
AC Q72W44;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=LIC_10096;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS68730.1; -; Genomic_DNA.
DR RefSeq; WP_000651373.1; NC_005823.1.
DR AlphaFoldDB; Q72W44; -.
DR SMR; Q72W44; -.
DR PaxDb; Q72W44; -.
DR EnsemblBacteria; AAS68730; AAS68730; LIC_10096.
DR GeneID; 61143452; -.
DR KEGG; lic:LIC_10096; -.
DR HOGENOM; CLU_075045_0_1_12; -.
DR OMA; YRQGIFP; -.
DR Proteomes; UP000007037; 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..219
FT /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT /id="PRO_0000207226"
SQ SEQUENCE 219 AA; 25596 MW; E461CFFE1B4FB575 CRC64;
MKDFSDFFRN PHIWDREIVA VGGDLSPERL LYAYKNGIFP WSDQPILWYC LDPRSIFDLN
KLHISKRLKR KINQKRYTIT FNRAFEQVMR CCAYRPGEDT WITDLFIKSY TEFHKLGYAH
SLEVWDENGK LGGGVYGIAI GNFFAGESMF SFIPDFGKIG LFHLFETLKK DHFTLFDTQQ
LNLVTLSLGA YQIPKKEYLK RLESAVASGK KWNPSHFVL