LFTR_PSEP1
ID LFTR_PSEP1 Reviewed; 226 AA.
AC A5W1H1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=Pput_1828;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ77981.1; -; Genomic_DNA.
DR RefSeq; WP_003251213.1; NC_009512.1.
DR AlphaFoldDB; A5W1H1; -.
DR SMR; A5W1H1; -.
DR STRING; 351746.Pput_1828; -.
DR EnsemblBacteria; ABQ77981; ABQ77981; Pput_1828.
DR KEGG; ppf:Pput_1828; -.
DR eggNOG; COG2360; Bacteria.
DR HOGENOM; CLU_075045_0_0_6; -.
DR OMA; YRQGIFP; -.
DR OrthoDB; 1670846at2; -.
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..226
FT /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT /id="PRO_1000045112"
SQ SEQUENCE 226 AA; 25194 MW; 260CB53304D496D7 CRC64;
MLTWLTRDSL TFPPLEKALH DPNGLLAAGG DLSPERLVQA YRHGCFPWYQ DGQPILWWSP
DPRTVLLPDQ LHVSRSLAKL MRQGRYQVSF DTDFPAVIAA CAAPRDYADG TWITDTMRNA
YCELHRRGIA HSVEVRQDGE LVGGLYGLAM GQLFFGESMF SRADNASKVG FVTLVNHLRD
AGFVLIDCQM PTNHLHSLGA HAISRAEFAS YLARHLDQPN SASWVA