TPX_BACSU
ID TPX_BACSU Reviewed; 167 AA.
AC P80864;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
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=ytgI;
GN OrderedLocusNames=BSU29490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-32.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [4]
RP STRUCTURE BY NMR OF 1-167, AND DISULFIDE BOND.
RX PubMed=18588855; DOI=10.1016/j.bbrc.2008.06.051;
RA Lu J., Yang F., Li Y., Zhang X., Xia B., Jin C.;
RT "Reversible conformational switch revealed by the redox structures of
RT Bacillus subtilis thiol peroxidase.";
RL Biochem. Biophys. Res. Commun. 373:414-418(2008).
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. {ECO:0000255|HAMAP-Rule:MF_00269}.
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};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269}.
CC -!- INDUCTION: By superoxide.
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 -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00269}.
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DR EMBL; AF008220; AAC00316.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14927.1; -; Genomic_DNA.
DR PIR; F69992; F69992.
DR RefSeq; NP_390827.1; NC_000964.3.
DR RefSeq; WP_003223506.1; NZ_JNCM01000036.1.
DR PDB; 2JSY; NMR; -; A=1-167.
DR PDB; 2JSZ; NMR; -; A=1-167.
DR PDBsum; 2JSY; -.
DR PDBsum; 2JSZ; -.
DR AlphaFoldDB; P80864; -.
DR BMRB; P80864; -.
DR SMR; P80864; -.
DR IntAct; P80864; 1.
DR MINT; P80864; -.
DR STRING; 224308.BSU29490; -.
DR jPOST; P80864; -.
DR PaxDb; P80864; -.
DR PRIDE; P80864; -.
DR EnsemblBacteria; CAB14927; CAB14927; BSU_29490.
DR GeneID; 64304667; -.
DR GeneID; 937688; -.
DR KEGG; bsu:BSU29490; -.
DR PATRIC; fig|224308.179.peg.3204; -.
DR eggNOG; COG2077; Bacteria.
DR InParanoid; P80864; -.
DR OMA; ITQEPNY; -.
DR PhylomeDB; P80864; -.
DR BioCyc; BSUB:BSU29490-MON; -.
DR EvolutionaryTrace; P80864; -.
DR PRO; PR:P80864; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
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; Direct protein sequencing; Disulfide bond;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659"
FT CHAIN 2..167
FT /note="Thiol peroxidase"
FT /id="PRO_0000187870"
FT DOMAIN 18..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT ACT_SITE 60
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269,
FT ECO:0000305|PubMed:18588855"
FT DISULFID 60..94
FT /note="Redox active"
FT /evidence="ECO:0000269|PubMed:18588855,
FT ECO:0007744|PDB:2JSY"
FT DISULFID 60..94
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2JSZ"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:2JSY"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2JSY"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2JSY"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:2JSY"
SQ SEQUENCE 167 AA; 18216 MW; 5B2BD8169C0555C6 CRC64;
MAEITFKGGP VTLVGQEVKV GDQAPDFTVL TNSLEEKSLA DMKGKVTIIS VIPSIDTGVC
DAQTRRFNEE AAKLGDVNVY TISADLPFAQ ARWCGANGID KVETLSDHRD MSFGEAFGVY
IKELRLLARS VFVLDENGKV VYAEYVSEAT NHPNYEKPIE AAKALVK
