Leucyl/phenylalanyl-tRNA--protein transferase

Details

Name
Leucyl/phenylalanyl-tRNA--protein transferase
Synonyms
  • 2.3.2.6
  • L/F-transferase
  • Leucyltransferase
  • Phenyalanyltransferase
  • ycaA
Gene Name
aat
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0013015|Leucyl/phenylalanyl-tRNA--protein transferase
MRLVQLSRHSIAFPSPEGALREPNGLLALGGDLSPARLLMAYQRGIFPWFSPGDPILWWS
PDPRAVLWPESLHISRSMKRFHKRSPYRVTMNYAFGQVIEGCASDREEGTWITRGVVEAY
HRLHELGHAHSIEVWREDELVGGMYGVAQGTLFCGESMFSRMENASKTALLVFCEEFIGH
GGKLIDCQVLNDHTASLGACEIPRRDYLNYLNQMRLGRLPNNFWVPRCLFSPQE
Number of residues
234
Molecular Weight
26618.275
Theoretical pI
7.25
GO Classification
Functions
leucyltransferase activity / transferase activity, transferring amino-acyl groups
Processes
protein catabolic process
Components
cytoplasm
General Function
Transferase activity, transferring amino-acyl groups
Specific Function
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0013016|Leucyl/phenylalanyl-tRNA--protein transferase (aat)
ATGCGCCTGGTTCAGCTTTCTCGCCATTCAATAGCCTTCCCTTCCCCGGAAGGCGCATTA
CGTGAGCCTAACGGCCTGCTGGCACTTGGGGGCGATCTTAGCCCTGCGCGCCTGTTAATG
GCTTACCAGCGTGGTATTTTTCCGTGGTTTTCTCCAGGCGACCCCATCCTCTGGTGGTCG
CCCGATCCCCGCGCGGTGCTATGGCCAGAATCACTGCATATCAGCCGTAGTATGAAGCGA
TTTCATAAACGCTCGCCCTATCGTGTCACGATGAATTACGCTTTTGGTCAGGTCATTGAA
GGCTGTGCCAGCGATCGCGAAGAAGGAACCTGGATCACGCGTGGCGTGGTCGAAGCCTAC
CATCGCCTTCACGAACTCGGCCATGCCCACTCCATTGAAGTCTGGCGTGAAGATGAGCTT
GTCGGCGGTATGTACGGCGTGGCCCAGGGAACGCTATTTTGTGGCGAGTCCATGTTCAGC
CGGATGGAAAATGCGTCTAAAACGGCGCTTCTGGTATTCTGTGAGGAATTTATCGGTCAT
GGCGGTAAGCTTATCGACTGCCAGGTCCTTAACGATCACACAGCATCGCTTGGTGCCTGC
GAAATTCCCCGCCGGGATTACCTTAATTATCTCAATCAAATGCGCCTCGGACGATTGCCG
AATAATTTCTGGGTACCACGATGCTTGTTTTCACCACAAGAATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A8P1
UniProtKB Entry NameLFTR_ECOLI
GenBank Protein ID146480
GenBank Gene IDM63145
General References
  1. Cummings HS, Sands JF, Foreman PC, Fraser J, Hershey JW: Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate. J Biol Chem. 1991 Sep 5;266(25):16491-8. [Article]
  2. Shrader TE, Tobias JW, Varshavsky A: The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat. J Bacteriol. 1993 Jul;175(14):4364-74. [Article]
  3. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Abramochkin G, Shrader TE: The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure. J Biol Chem. 1995 Sep 1;270(35):20621-8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08437PuromycinexperimentalunknownDetails