P0A8P1 (LFTR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
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.
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 Reference proteome
Gene Ontology (GO)
Biological process	protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	leucyltransferase activity Inferred from electronic annotation. Source: EC
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 [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

EMBL
GenBank
DDBJ

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

NP_415405.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A8P1.

SMR

P0A8P1. Positions 2-233.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48235N.

IntAct

P0A8P1. 8 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002220; EBESCP00000002220; EBESCG00000001820.
EBESCT00000017409; EBESCP00000016700; EBESCG00000016465.

GeneID

945490.

GenomeReviews

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

KEGG

ecj:JW0868.
eco:b0885.

PATRIC

32116979. VBIEscCol129921_0914.

Organism-specific databases

EchoBASE

EB1103.

EcoGene

EG11112. aat.

Phylogenomic databases

eggNOG

COG2360.

GeneTree

EBGT00050000011414.

HOGENOM

HBG485363.

OMA

GEPILWW.

PhylomeDB

P0A8P1.

ProtClustDB

PRK00301.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11112-MONOMER.
MetaCyc:EG11112-MONOMER.

Gene expression databases

Genevestigator

P0A8P1.

Family and domain databases

HAMAP

MF_00688. Leu_Phe_trans.
[Tree]

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]

KO

K00684.

Pfam

PF03588. Leu_Phe_trans. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.

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:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program