Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiol peroxidase

Gene

tpx

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has antioxidant activity. Could remove peroxides or H2O2 within the catalase- and peroxidase-deficient periplasmic space.

GO - Molecular functioni

  • hydroperoxide reductase activity Source: EcoCyc
  • thioredoxin peroxidase activity Source: EcoCyc

GO - Biological processi

  • cell redox homeostasis Source: UniProtKB-HAMAP
  • cellular oxidant detoxification Source: GOC
  • cellular response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciEcoCyc:G6660-MONOMER.
ECOL316407:JW1317-MONOMER.
MetaCyc:G6660-MONOMER.
BRENDAi1.11.1.7. 2026.

Protein family/group databases

PeroxiBasei6007. EcoTPx.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol peroxidase (EC:1.11.1.-)
Alternative name(s):
Scavengase P20
Gene namesi
Name:tpx
Synonyms:yzzJ
Ordered Locus Names:b1324, JW1317
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12672. tpx.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
  • periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 168167Thiol peroxidasePRO_0000187877Add
BLAST

Proteomic databases

EPDiP0A862.
PaxDbiP0A862.
PRIDEiP0A862.

2D gel databases

SWISS-2DPAGEP0A862.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ycfPP0A8E13EBI-369411,EBI-9129402

Protein-protein interaction databases

BioGridi4260151. 128 interactions.
850247. 1 interaction.
DIPiDIP-31857N.
IntActiP0A862. 9 interactions.
STRINGi511145.b1324.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi10 – 145Combined sources
Beta strandi29 – 313Combined sources
Beta strandi37 – 393Combined sources
Helixi40 – 434Combined sources
Beta strandi46 – 527Combined sources
Beta strandi56 – 594Combined sources
Helixi61 – 7111Combined sources
Helixi72 – 743Combined sources
Beta strandi75 – 8612Combined sources
Helixi88 – 9811Combined sources
Beta strandi102 – 1076Combined sources
Helixi112 – 1176Combined sources
Turni126 – 1294Combined sources
Beta strandi133 – 1386Combined sources
Beta strandi142 – 1498Combined sources
Helixi159 – 1646Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXHX-ray2.20A/B2-168[»]
3HVSX-ray1.80A/B2-168[»]
3HVVX-ray1.75A2-168[»]
3HVXX-ray2.12A/B/C/D2-168[»]
3I43X-ray2.80A/B2-168[»]
4AF2X-ray1.97A1-168[»]
ProteinModelPortaliP0A862.
SMRiP0A862. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A862.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 168150ThioredoxinAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family. Tpx subfamily.Curated
Contains 1 thioredoxin domain.Curated

Phylogenomic databases

eggNOGiENOG4108V1J. Bacteria.
COG2077. LUCA.
HOGENOMiHOG000022345.
InParanoidiP0A862.
KOiK11065.
OMAiKFNAQAN.
OrthoDBiEOG6NWBV8.
PhylomeDBiP0A862.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_00269. Tpx.
InterProiIPR002065. Put_TPX.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR018219. Tpx_CS.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
PS01265. TPX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A862-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL
60 70 80 90 100
NIFPSIDTGV CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL
110 120 130 140 150
NNVITLSTFR NAEFLQAYGV AIADGPLKGL AARAVVVIDE NDNVIFSQLV
160
DEITTEPDYE AALAVLKA
Length:168
Mass (Da):17,835
Last modified:January 23, 2007 - v2
Checksum:iF95F39094A07DBB2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611C → Y in AAC43517 (PubMed:7499381).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33213 Genomic DNA. Translation: AAC43517.1.
U93212 Genomic DNA. Translation: AAC45284.1.
U00096 Genomic DNA. Translation: AAC74406.1.
AP009048 Genomic DNA. Translation: BAA14906.1.
PIRiJC5504.
RefSeqiNP_415840.1. NC_000913.3.
WP_000084387.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74406; AAC74406; b1324.
BAA14906; BAA14906; BAA14906.
GeneIDi945880.
KEGGiecj:JW1317.
eco:b1324.
PATRICi32117922. VBIEscCol129921_1381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33213 Genomic DNA. Translation: AAC43517.1.
U93212 Genomic DNA. Translation: AAC45284.1.
U00096 Genomic DNA. Translation: AAC74406.1.
AP009048 Genomic DNA. Translation: BAA14906.1.
PIRiJC5504.
RefSeqiNP_415840.1. NC_000913.3.
WP_000084387.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXHX-ray2.20A/B2-168[»]
3HVSX-ray1.80A/B2-168[»]
3HVVX-ray1.75A2-168[»]
3HVXX-ray2.12A/B/C/D2-168[»]
3I43X-ray2.80A/B2-168[»]
4AF2X-ray1.97A1-168[»]
ProteinModelPortaliP0A862.
SMRiP0A862. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260151. 128 interactions.
850247. 1 interaction.
DIPiDIP-31857N.
IntActiP0A862. 9 interactions.
STRINGi511145.b1324.

Protein family/group databases

PeroxiBasei6007. EcoTPx.

2D gel databases

SWISS-2DPAGEP0A862.

Proteomic databases

EPDiP0A862.
PaxDbiP0A862.
PRIDEiP0A862.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74406; AAC74406; b1324.
BAA14906; BAA14906; BAA14906.
GeneIDi945880.
KEGGiecj:JW1317.
eco:b1324.
PATRICi32117922. VBIEscCol129921_1381.

Organism-specific databases

EchoBASEiEB2538.
EcoGeneiEG12672. tpx.

Phylogenomic databases

eggNOGiENOG4108V1J. Bacteria.
COG2077. LUCA.
HOGENOMiHOG000022345.
InParanoidiP0A862.
KOiK11065.
OMAiKFNAQAN.
OrthoDBiEOG6NWBV8.
PhylomeDBiP0A862.

Enzyme and pathway databases

BioCyciEcoCyc:G6660-MONOMER.
ECOL316407:JW1317-MONOMER.
MetaCyc:G6660-MONOMER.
BRENDAi1.11.1.7. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A862.
PROiP0A862.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_00269. Tpx.
InterProiIPR002065. Put_TPX.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR018219. Tpx_CS.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
PS01265. TPX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Thioredoxin-linked 'thiol peroxidase' from periplasmic space of Escherichia coli."
    Cha M.-K., Kim H.-K., Kim I.-H.
    J. Biol. Chem. 270:28635-28641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12.
  2. Zhou Y., Wan X.Y., Wang H.L., Yan Z.Y., Hou Y.D., Jin D.Y.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / DH5-alpha.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: PROTEIN SEQUENCE OF 2-19.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.
    Strain: K12 / EMG2.

Entry informationi

Entry nameiTPX_ECOLI
AccessioniPrimary (citable) accession number: P0A862
Secondary accession number(s): P37901
, P57669, P76047, P77786
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.