BCP_ECOLI
ID BCP_ECOLI Reviewed; 156 AA.
AC P0AE52; P23480;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Peroxiredoxin Bcp;
DE EC=1.11.1.24 {ECO:0000269|PubMed:10644761, ECO:0000269|PubMed:21910476};
DE AltName: Full=Bacterioferritin comigratory protein;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000305};
GN Name=bcp; OrderedLocusNames=b2480, JW2465;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2016588; DOI=10.1099/00221287-137-2-361;
RA Andrews S.C., Harrison P.M., Guest J.R.;
RT "A molecular analysis of the 53.3 minute region of the Escherichia coli
RT linkage map.";
RL J. Gen. Microbiol. 137:361-367(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC STRAIN=K12;
RX PubMed=9537378; DOI=10.1128/jb.180.7.1803-1807.1998;
RA Ghrist A.C., Stauffer G.V.;
RT "Promoter characterization and constitutive expression of the Escherichia
RT coli gcvR gene.";
RL J. Bacteriol. 180:1803-1807(1998).
RN [6]
RP PROTEIN SEQUENCE OF 1-15.
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 [7]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [8]
RP CATALYTIC ACTIVITY, ENZYME KINETICS, AND ACTIVE SITE.
RX PubMed=10644761; DOI=10.1074/jbc.275.4.2924;
RA Jeong W., Cha M.K., Kim I.H.;
RT "Thioredoxin-dependent hydroperoxide peroxidase activity of
RT bacterioferritin comigratory protein (BCP) as a new member of the thiol-
RT specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC)
RT family.";
RL J. Biol. Chem. 275:2924-2930(2000).
RN [9]
RP ACTIVE SITE, AND DISULFIDE BOND.
RX PubMed=19298085; DOI=10.1021/bi900189e;
RA Clarke D.J., Mackay C.L., Campopiano D.J., Langridge-Smith P., Brown A.R.;
RT "Interrogating the molecular details of the peroxiredoxin activity of the
RT Escherichia coli bacterioferritin comigratory protein using high-resolution
RT mass spectrometry.";
RL Biochemistry 48:3904-3914(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=21910476; DOI=10.1021/bi200935d;
RA Reeves S.A., Parsonage D., Nelson K.J., Poole L.B.;
RT "Kinetic and thermodynamic features reveal that Escherichia coli BCP is an
RT unusually versatile peroxiredoxin.";
RL Biochemistry 50:8970-8981(2011).
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:0000269|PubMed:21910476}.
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:0000269|PubMed:10644761, ECO:0000269|PubMed:21910476};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76.1 uM for H(2)O(2) (using glutathione Grx1 as electron donor)
CC {ECO:0000269|PubMed:21910476};
CC KM=99.5 uM for cumene hydroperoxide (using glutathione Grx1 as
CC electron donor) {ECO:0000269|PubMed:21910476};
CC KM=6800 uM for tert-butyl hydroperoxide (using glutathione Grx1 as
CC electron donor) {ECO:0000269|PubMed:21910476};
CC KM=14.6 uM for H(2)O(2) (using thioredoxin Trx1 as electron donor)
CC {ECO:0000269|PubMed:21910476};
CC KM=21.6 uM for cumene hydroperoxide (using thioredoxin Trx1 as
CC electron donor) {ECO:0000269|PubMed:21910476};
CC KM=574 uM for tert-butyl hydroperoxide (using thioredoxin Trx1 as
CC electron donor) {ECO:0000269|PubMed:21910476};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21910476}.
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:0000305|PubMed:19298085}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; M63654; AAB88562.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75533.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16358.1; -; Genomic_DNA.
DR EMBL; AF023337; AAC46233.1; -; Genomic_DNA.
DR PIR; B49749; B49749.
DR RefSeq; NP_416975.1; NC_000913.3.
DR RefSeq; WP_001068682.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0AE52; -.
DR SMR; P0AE52; -.
DR BioGRID; 4260768; 41.
DR BioGRID; 851288; 2.
DR IntAct; P0AE52; 7.
DR STRING; 511145.b2480; -.
DR SWISS-2DPAGE; P0AE52; -.
DR jPOST; P0AE52; -.
DR PaxDb; P0AE52; -.
DR PRIDE; P0AE52; -.
DR EnsemblBacteria; AAC75533; AAC75533; b2480.
DR EnsemblBacteria; BAA16358; BAA16358; BAA16358.
DR GeneID; 66673655; -.
DR GeneID; 946949; -.
DR KEGG; ecj:JW2465; -.
DR KEGG; eco:b2480; -.
DR PATRIC; fig|1411691.4.peg.4259; -.
DR EchoBASE; EB0106; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_042529_14_1_6; -.
DR InParanoid; P0AE52; -.
DR OMA; RVVVYFY; -.
DR PhylomeDB; P0AE52; -.
DR BioCyc; EcoCyc:EG10108-MON; -.
DR BioCyc; MetaCyc:EG10108-MON; -.
DR BRENDA; 1.11.1.24; 2026.
DR PRO; PR:P0AE52; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:EcoCyc.
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 GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
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 Antioxidant; Direct protein sequencing; Disulfide bond; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..156
FT /note="Peroxiredoxin Bcp"
FT /id="PRO_0000135134"
FT DOMAIN 4..156
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000269|PubMed:10644761,
FT ECO:0000269|PubMed:19298085"
FT DISULFID 46..51
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:19298085"
SQ SEQUENCE 156 AA; 17634 MW; C7D267A671409EFC CRC64;
MNPLKAGDIA PKFSLPDQDG EQVNLTDFQG QRVLVYFYPK AMTPGCTVQA CGLRDNMDEL
KKAGVDVLGI STDKPEKLSR FAEKELLNFT LLSDEDHQVC EQFGVWGEKS FMGKTYDGIH
RISFLIDADG KIEHVFDDFK TSNHHDVVLN WLKEHA
