Reviewed, UniProtKB/Swiss-Prot P0A8P1 (LFTR_ECOLI)

Names and origin

Protein names

Recommended name:
    Leucyl/phenylalanyl-tRNA--protein transferase
    EC=2.3.2.6
Alternative name(s):
    L/F-transferase
    Leucyltransferase
    Phenyalanyltransferase

Gene names

Name:	aat
Synonyms:	ycaA
Ordered Locus Names:	b0885, JW0868

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. HAMAP MF_00688
Catalytic activity	L-leucyl-tRNA + protein = tRNA + L-leucyl-protein. HAMAP MF_00688 L-phenylalanyl-tRNA + protein = tRNA + L-phenylalanyl-protein. HAMAP MF_00688
Subunit structure	Monomer. HAMAP MF_00688
Subcellular location	Cytoplasm. HAMAP MF_00688
Sequence similarities	Belongs to the L/F-transferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW leucyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 234

234

Leucyl/phenylalanyl-tRNA--protein transferase HAMAP MF_00688

PRO_0000207217

Secondary structure

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234

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

16 – 18

3

Turn

21 – 25

5

Beta strand

26 – 29

4

Helix

35 – 43

9

Beta strand

57 – 59

3

Beta strand

62 – 67

6

Helix

69 – 71

3

Helix

76 – 83

8

Beta strand

88 – 93

6

Helix

95 – 103

9

Helix

114 – 125

12

Beta strand

128 – 136

9

Beta strand

139 – 149

11

Beta strand

152 – 162

11

Helix

165 – 179

15

Beta strand

184 – 189

6

Helix

192 – 196

5

Beta strand

200 – 202

3

Helix

204 – 214

11

Turn

221 – 224

4

Beta strand

225 – 230

6

Sequences

	Sequence		Length	Mass (Da)
	P0A8P1-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 8C725890D42ABF6F	FASTA	234	26,619
	10 20 30 40 50 60 MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF SPGDPILWWS 70 80 90 100 110 120 PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE GCASDREEGT WITRGVVEAY 130 140 150 160 170 180 HRLHELGHAH SIEVWREDEL VGGMYGVAQG TLFCGESMFS RMENASKTAL LVFCEEFIGH 190 200 210 220 230 GGKLIDCQVL NDHTASLGAC EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate." Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B. J. Biol. Chem. 266:16491-16498(1991) [PubMed: 1909328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat." Shrader T.E., Tobias J.W., Varshavsky A. J. Bacteriol. 175:4364-4374(1993) [PubMed: 8331068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[3]	"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." 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., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure." Abramochkin G., Shrader T.E. J. Biol. Chem. 270:20621-20628(1995) [PubMed: 7657641] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M63145 Genomic DNA. Translation: AAC36910.1.
L10383 Unassigned DNA. Translation: AAA03231.1.
U00096 Genomic DNA. Translation: AAC73971.1.
AP009048 Genomic DNA. Translation: BAA35605.1.

PIR

A36888.

RefSeq

AP_001515.1.
NP_415405.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CXA	X-ray	1.60	A	1-234	[»]
2DPS	X-ray	2.40	A/B	1-234	[»]
2DPT	X-ray	2.75	A/B	1-234	[»]
2Z3K	X-ray	2.85	A/B	2-234	[»]
2Z3L	X-ray	2.75	A/B	2-234	[»]
2Z3M	X-ray	2.70	A/B	2-234	[»]
2Z3N	X-ray	2.50	A/B	2-234	[»]
2Z3O	X-ray	2.40	A/B	2-234	[»]
2Z3P	X-ray	2.50	A/B	2-234	[»]

ModBase

Search...

Genome annotation databases

GeneID

945490.

GenomeReviews

Gene locus JW0868 in contig AP009048_GR.
Gene locus b0885 in contig U00096_GR.

KEGG

ecj:JW0868.
eco:b0885.

Organism-specific databases

EchoBASE

EB1103.

EcoGene

EG11112. aat.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A8P1.

OMA

P0A8P1. MFYGESM.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11112-MON.

Family and domain databases

HAMAP

MF_00688.
[Tree]

InterPro

IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]

Pfam

PF03588. Leu_Phe_trans. 1 hit.
[Graphical view]

ProDom

PD022844. Aat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00667. aat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

LFTR_ECOLI

Accession

Primary (citable) accession number: P0A8P1
Secondary accession number(s): P23885

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)