P0A7D1 (PTH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-tRNA hydrolase
Short name=PTH
EC=3.1.1.29

Gene names

Name:	pth
Ordered Locus Names:	b1204, JW1195

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death. HAMAP-Rule MF_00083
Catalytic activity	N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA. HAMAP-Rule MF_00083
Subunit structure	Monomer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00083.
Sequence similarities	Belongs to the PTH family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	misfolded or incompletely synthesized protein catabolic process Inferred from direct assay PubMed 10049395PubMed 10452886. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aminoacyl-tRNA hydrolase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
prs	P0A717	1	EBI-556507,EBI-906827

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 194

194

Peptidyl-tRNA hydrolase HAMAP-Rule MF_00083

PRO_0000187733

Experimental info

Mutagenesis

101

1

G → D: Pth(ts) mutants synthesize thermosensitive PTH and die at 42 degrees Celsius from a defect in protein synthesis.

Mutagenesis

134

1

R → H: Rap mutants do not support vegetative growth of bacteriophage lambda and die upon transcription of lambda DNA bar sites.

Secondary structure

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194

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Turn

14 – 18

5

Helix

20 – 22

3

Helix

23 – 35

13

Beta strand

40 – 42

3

Helix

43 – 45

3

Beta strand

47 – 54

8

Beta strand

57 – 64

8

Helix

68 – 71

4

Helix

72 – 82

11

Helix

86 – 88

3

Beta strand

89 – 95

7

Beta strand

103 – 108

6

Helix

115 – 123

9

Beta strand

130 – 136

7

Helix

143 – 150

8

Helix

156 – 179

24

Helix

181 – 190

10

Turn

191 – 193

3

Sequences

	Sequence		Length	Mass (Da)
	P0A7D1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: A28A69A63F2DD530	FASTA	194	21,082
	10 20 30 40 50 60 MTIKLIVGLA NPGAEYAATR HNAGAWFVDL LAERLRAPLR EEAKFFGYTS RVTLGGEDVR 70 80 90 100 110 120 LLVPTTFMNL SGKAVAAMAS FFRINPDEIL VAHDELDLPP GVAKFKLGGG HGGHNGLKDI 130 140 150 160 170 180 ISKLGNNPNF HRLRIGIGHP GDKNKVVGFV LGKPPVSEQK LIDEAIDEAA RCTEMWFTDG 190 LTKATNRLHA FKAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis." Garcia-Villegas M.R., de la Vega F.M., Galindo J.M., Segura M., Buckingham R.H., Guarneros G. EMBO J. 10:3549-3555(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17. Strain: K12.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase." Schmitt E., Fromant M., Plateau P., Mechulam Y., Blanquet S. Proteins 28:135-136(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION.
[6]	"Crystal structure at 1.2-A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase." Schmitt E., Mechulam Y., Fromant M., Plateau P., Blanquet S. EMBO J. 16:4760-4769(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X61941 Genomic DNA. Translation: CAA43945.1.
U00096 Genomic DNA. Translation: AAC74288.1.
AP009048 Genomic DNA. Translation: BAA36062.1.

PIR

S16753.

RefSeq

NP_415722.1. NC_000913.2.
YP_489471.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PTH	X-ray	1.20	A	2-194	[»]
3VJR	X-ray	2.40	A/C	1-194	[»]

ProteinModelPortal

P0A7D1.

SMR

P0A7D1. Positions 2-194.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35932N.

IntAct

P0A7D1. 15 interactions.

MINT

MINT-1225563.

STRING

511145.b1204.

Proteomic databases

PaxDb

P0A7D1.

PRIDE

P0A7D1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74288; AAC74288; b1204.
BAA36062; BAA36062; BAA36062.

GeneID

12933876.
945765.

KEGG

ecj:Y75_p1176.
eco:b1204.

PATRIC

32117660. VBIEscCol129921_1252.

Organism-specific databases

EchoBASE

EB0778.

EcoGene

EG10785. pth.

Phylogenomic databases

eggNOG

COG0193.

HOGENOM

HOG000004796.

KO

K01056.

OMA

IKFKTGG.

ProtClustDB

PRK05426.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10785-MONOMER.
ECOL316407:JW1195-MONOMER.
MetaCyc:EG10785-MONOMER.

SABIO-RK

P0A7D1.

Gene expression databases

Genevestigator

P0A7D1.

Family and domain databases

Gene3D

3.40.50.1470. 1 hit.

HAMAP

MF_00083. Pept_tRNA_hydro_bact.

InterPro

IPR001328. Pept_tRNA_hydro.
IPR018171. Pept_tRNA_hydro_CS.
[Graphical view]

PANTHER

PTHR17224. PTHR17224. 1 hit.

Pfam

PF01195. Pept_tRNA_hydro. 1 hit.
[Graphical view]

SUPFAM

SSF53178. Pept_tRNA_hydro. 1 hit.

TIGRFAMs

TIGR00447. pth. 1 hit.

PROSITE

PS01195. PEPT_TRNA_HYDROL_1. 1 hit.
PS01196. PEPT_TRNA_HYDROL_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7D1.

Entry information

Entry name

PTH_ECOLI

Accession

Primary (citable) accession number: P0A7D1
Secondary accession number(s): P23932

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program