TPX_ECOLI
ID TPX_ECOLI Reviewed; 168 AA.
AC P0A862; P37901; P57669; P76047; P77786;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000303|PubMed:7499381};
DE Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:12514184};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Scavengase p20 {ECO:0000303|PubMed:9168946};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; Synonyms=yzzJ;
GN OrderedLocusNames=b1324, JW1317;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=7499381; DOI=10.1074/jbc.270.48.28635;
RA Cha M.-K., Kim H.-K., Kim I.-H.;
RT "Thioredoxin-linked 'thiol peroxidase' from periplasmic space of
RT Escherichia coli.";
RL J. Biol. Chem. 270:28635-28641(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / DH5-alpha;
RX PubMed=9168946; DOI=10.1006/bbrc.1997.6564;
RA Zhou Y., Wan X.Y., Wang H.L., Yan Z.Y., Hou Y.D., Jin D.Y.;
RT "Bacterial scavengase p20 is structurally and functionally related to
RT peroxiredoxins.";
RL Biochem. Biophys. Res. Commun. 233:848-852(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-19.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP AND MUTAGENESIS OF CYS-61; CYS-82 AND CYS-95.
RX PubMed=12514184; DOI=10.1074/jbc.m209888200;
RA Baker L.M., Poole L.B.;
RT "Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic
RT acid formation and overoxidation of essential CYS61.";
RL J. Biol. Chem. 278:9203-9211(2003).
RN [9]
RP FUNCTION.
RX PubMed=14676195; DOI=10.1074/jbc.m312388200;
RA Cha M.K., Kim W.C., Lim C.J., Kim K., Kim I.H.;
RT "Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide
RT peroxidase and the principal antioxidative function during anaerobic
RT growth.";
RL J. Biol. Chem. 279:8769-8778(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19054092; DOI=10.1111/j.1574-6968.2008.01372.x;
RA Tao K.;
RT "Subcellular localization and in vivo oxidation-reduction kinetics of thiol
RT peroxidase in Escherichia coli.";
RL FEMS Microbiol. Lett. 289:41-45(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=14506251; DOI=10.1074/jbc.m309015200;
RA Choi J., Choi S., Choi J., Cha M.K., Kim I.H., Shin W.;
RT "Crystal structure of Escherichia coli thiol peroxidase in the oxidized
RT state: insights into intramolecular disulfide formation and substrate
RT binding in atypical 2-Cys peroxiredoxins.";
RL J. Biol. Chem. 278:49478-49486(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), DISULFIDE BOND, AND SUBUNIT.
RX PubMed=19699750; DOI=10.1016/j.jmb.2009.08.040;
RA Hall A., Sankaran B., Poole L.B., Karplus P.A.;
RT "Structural changes common to catalysis in the Tpx peroxiredoxin
RT subfamily.";
RL J. Mol. Biol. 393:867-881(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 1-168.
RX PubMed=22691780; DOI=10.1107/s1744309112011487;
RA Beckham K.S., Byron O., Roe A.J., Gabrielsen M.;
RT "The structure of an orthorhombic crystal form of a 'forced reduced' thiol
RT peroxidase reveals lattice formation aided by the presence of the affinity
RT tag.";
RL Acta Crystallogr. F 68:522-526(2012).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. Has a preference for alkyl hydroperoxides and
CC acts as lipid peroxidase to inhibit bacterial membrane oxidation. Acts
CC as principal antioxidant during anaerobic growth. {ECO:0000255|HAMAP-
CC Rule:MF_00269, ECO:0000269|PubMed:12514184,
CC ECO:0000269|PubMed:14676195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00269, ECO:0000269|PubMed:12514184};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1730 uM for H(2)O(2) {ECO:0000269|PubMed:12514184};
CC KM=9.1 uM for cumene hydroperoxide {ECO:0000269|PubMed:12514184};
CC KM=25.5 uM for Trx1 (using H(2)O(2) as substrate)
CC {ECO:0000269|PubMed:12514184};
CC KM=22.5 uM for Trx1 (using cumene hydroperoxide as substrate)
CC {ECO:0000269|PubMed:12514184};
CC Note=kcat is 76.0 sec(-1) with H(2)O(2) as substrate and 70.1 sec(-1)
CC with cumene hydroperoxide as substrate.
CC {ECO:0000269|PubMed:12514184};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269,
CC ECO:0000269|PubMed:19699750}.
CC -!- INTERACTION:
CC P0A862; P0A8E1: ycfP; NbExp=3; IntAct=EBI-369411, EBI-9129402;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7499381}. Cytoplasm
CC {ECO:0000269|PubMed:19054092}. Note=Forms a mixed disulfide with
CC cytoplasmic thioredoxin (trx1). {ECO:0000269|PubMed:19054092}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000255|HAMAP-Rule:MF_00269,
CC ECO:0000305|PubMed:12514184}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33213; AAC43517.1; -; Genomic_DNA.
DR EMBL; U93212; AAC45284.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74406.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14906.1; -; Genomic_DNA.
DR PIR; JC5504; JC5504.
DR RefSeq; NP_415840.1; NC_000913.3.
DR RefSeq; WP_000084387.1; NZ_STEB01000005.1.
DR PDB; 1QXH; X-ray; 2.20 A; A/B=2-168.
DR PDB; 3HVS; X-ray; 1.80 A; A/B=2-168.
DR PDB; 3HVV; X-ray; 1.75 A; A=2-168.
DR PDB; 3HVX; X-ray; 2.12 A; A/B/C/D=2-168.
DR PDB; 3I43; X-ray; 2.80 A; A/B=2-168.
DR PDB; 4AF2; X-ray; 1.97 A; A=1-168.
DR PDBsum; 1QXH; -.
DR PDBsum; 3HVS; -.
DR PDBsum; 3HVV; -.
DR PDBsum; 3HVX; -.
DR PDBsum; 3I43; -.
DR PDBsum; 4AF2; -.
DR AlphaFoldDB; P0A862; -.
DR SMR; P0A862; -.
DR BioGRID; 4260151; 139.
DR BioGRID; 850247; 3.
DR DIP; DIP-31857N; -.
DR IntAct; P0A862; 9.
DR STRING; 511145.b1324; -.
DR PeroxiBase; 6007; EcoTPx.
DR SWISS-2DPAGE; P0A862; -.
DR jPOST; P0A862; -.
DR PaxDb; P0A862; -.
DR PRIDE; P0A862; -.
DR EnsemblBacteria; AAC74406; AAC74406; b1324.
DR EnsemblBacteria; BAA14906; BAA14906; BAA14906.
DR GeneID; 58461552; -.
DR GeneID; 945880; -.
DR KEGG; ecj:JW1317; -.
DR KEGG; eco:b1324; -.
DR PATRIC; fig|1411691.4.peg.954; -.
DR EchoBASE; EB2538; -.
DR eggNOG; COG2077; Bacteria.
DR InParanoid; P0A862; -.
DR OMA; ITQEPNY; -.
DR PhylomeDB; P0A862; -.
DR BioCyc; EcoCyc:G6660-MON; -.
DR BioCyc; MetaCyc:G6660-MON; -.
DR BRENDA; 1.11.1.7; 2026.
DR EvolutionaryTrace; P0A862; -.
DR PRO; PR:P0A862; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:EcoCyc.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR HAMAP; MF_00269; Tpx; 1.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002065; TPX.
DR InterPro; IPR018219; Tpx_CS.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Periplasm; Peroxidase; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646, ECO:0000269|Ref.6"
FT CHAIN 2..168
FT /note="Thiol peroxidase"
FT /id="PRO_0000187877"
FT DOMAIN 19..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 61
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269,
FT ECO:0000269|PubMed:12514184"
FT DISULFID 61..95
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269,
FT ECO:0000269|PubMed:14506251, ECO:0000269|PubMed:19699750,
FT ECO:0007744|PDB:1QXH, ECO:0007744|PDB:3HVS,
FT ECO:0007744|PDB:3I43"
FT MUTAGEN 61
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:12514184"
FT MUTAGEN 82
FT /note="C->S: Reduces catalytic activity by 28%."
FT /evidence="ECO:0000269|PubMed:12514184"
FT MUTAGEN 95
FT /note="C->S: Reduces catalytic activity by 80%."
FT /evidence="ECO:0000269|PubMed:12514184"
FT CONFLICT 61
FT /note="C -> Y (in Ref. 1; AAC43517)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3HVV"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3HVX"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:3HVV"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 75..86
FT /evidence="ECO:0007829|PDB:3HVV"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3HVV"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:3HVV"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3HVV"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:3HVV"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:3HVV"
SQ SEQUENCE 168 AA; 17835 MW; F95F39094A07DBB2 CRC64;
MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV
CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV
AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA
