ID   LFTR_PSYCK              Reviewed;         274 AA.
AC   Q1QDP2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   02-SEP-2026, entry version 98.
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};
GN   OrderedLocusNames=Pcryo_0428;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) 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=N-terminal L-lysyl-[protein] + L-leucyl-tRNA(Leu) = N-terminal
CC         L-leucyl-L-lysyl-[protein] + tRNA(Leu) + H(+); Xref=Rhea:RHEA:12340,
CC         Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622, Rhea:RHEA-COMP:12670,
CC         Rhea:RHEA-COMP:12671, ChEBI:CHEBI:15378, ChEBI:CHEBI:65249,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:133043; EC=2.3.2.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00688};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-arginyl-[protein] + L-leucyl-tRNA(Leu) = N-
CC         terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu) + H(+);
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=L-phenylalanyl-tRNA(Phe) + an N-terminal L-alpha-aminoacyl-
CC         [protein] = 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; CP000323; ABE74211.1; -; Genomic_DNA.
DR   RefSeq; WP_011512796.1; NC_007969.1.
DR   AlphaFoldDB; Q1QDP2; -.
DR   SMR; Q1QDP2; -.
DR   STRING; 335284.Pcryo_0428; -.
DR   KEGG; pcr:Pcryo_0428; -.
DR   eggNOG; COG2360; Bacteria.
DR   HOGENOM; CLU_075045_0_0_6; -.
DR   Proteomes; UP000002425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008914; F:leucyl-tRNA--protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.630.70; Leucyl/phenylalanyl-tRNA-protein transferase, C-terminal domain; 1.
DR   Gene3D; 3.30.70.3550; Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain; 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   InterPro; IPR063613; Leu_Phe_trans_N.
DR   NCBIfam; TIGR00667; aat; 1.
DR   PANTHER; PTHR30098; LEUCYL/PHENYLALANYL-TRNA--PROTEIN TRANSFERASE; 1.
DR   PANTHER; PTHR30098:SF2; LEUCYL_PHENYLALANYL-TRNA--PROTEIN TRANSFERASE; 1.
DR   Pfam; PF03588; Leu_Phe_trans; 1.
DR   Pfam; PF30046; Leu_Phe_trans_N; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..274
FT                   /note="Leucyl/phenylalanyl-tRNA--protein transferase"
FT                   /id="PRO_0000258082"
SQ   SEQUENCE   274 AA;  30622 MW;  B56B35607E99DE7A CRC64;
     MSDFVNDGHT TPEAFVQHIK SLGRYDFPEP AIVDPEGMGI VAIGGDLAPE TLISAYAQGL
     FPWFNDDEPI AWWCPEPRCV MQPTDYQPSK SLRKLANRSR WQLTLNQAFD EVIHACSLPR
     SNGVNNDLNE SQPVGEHTWI HDEMIEAYTE LHAQGFAHSI EVWDDKGALV GGLYGLKIGG
     IYFGESMFHI ASNASKLAFW GLMRLCEHSN VNLVDCQLPN DHLMSLGAIT LSRTEFLTQL
     DILISNSSDN WHKNSHKPLA VPLLGSLQPW QLNL
//