BCPB_MYCTU
ID BCPB_MYCTU Reviewed; 154 AA.
AC P9WID9; L0T7E6; O53911; Q7D8A1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Putative peroxiredoxin Rv1608c;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P0AE52};
DE AltName: Full=Bacterioferritin comigratory protein;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Rv1608c {ECO:0000305};
GN Name=bcpB; Synonyms=bcp1; OrderedLocusNames=Rv1608c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RA Abendroth J., Mayclin S.J., Lorimer D.D., Edwards T.E.;
RT "Crystal structure of peroxidoxin BcpB from Mycobacterium tuberculosis.";
RL Submitted (NOV-2015) to the PDB data bank.
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 and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000250|UniProtKB:P0AE52}.
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;
CC Evidence={ECO:0000250|UniProtKB:P0AE52};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AE52}.
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:0000250|UniProtKB:P0AE52}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44372.1; -; Genomic_DNA.
DR PIR; G70819; G70819.
DR RefSeq; NP_216124.1; NC_000962.3.
DR RefSeq; WP_003407974.1; NZ_NVQJ01000016.1.
DR PDB; 5EPF; X-ray; 1.35 A; A=1-154.
DR PDBsum; 5EPF; -.
DR AlphaFoldDB; P9WID9; -.
DR SMR; P9WID9; -.
DR STRING; 83332.Rv1608c; -.
DR PaxDb; P9WID9; -.
DR GeneID; 45425576; -.
DR GeneID; 885530; -.
DR KEGG; mtu:Rv1608c; -.
DR TubercuList; Rv1608c; -.
DR eggNOG; COG1225; Bacteria.
DR OMA; MNTHADR; -.
DR PhylomeDB; P9WID9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..154
FT /note="Putative peroxiredoxin Rv1608c"
FT /id="PRO_0000396097"
FT DOMAIN 1..153
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 44
FT /evidence="ECO:0000250"
FT ACT_SITE 44
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5EPF"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5EPF"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:5EPF"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:5EPF"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:5EPF"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5EPF"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5EPF"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5EPF"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:5EPF"
SQ SEQUENCE 154 AA; 16894 MW; 44E62411F90946CF CRC64;
MKTGDTVADF ELPDQTGTPR RLSVLLSDGP VVLFFYPAAM TPGCTKEACH FRDLAKEFAE
VRASRVGIST DPVRKQAKFA EVRRFDYPLL SDAQGTVAAQ FGVKRGLLGK LMPVKRTTFV
IDTDRKVLDV ISSEFSMDAH ADKALATLRA IRSG
