BCP_HAEIN
ID BCP_HAEIN Reviewed; 155 AA.
AC P44411;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative peroxiredoxin bcp;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P0AE52};
DE AltName: Full=Bacterioferritin comigratory protein homolog;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000305};
GN Name=bcp; OrderedLocusNames=HI_0254;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC21920.1; -; Genomic_DNA.
DR PIR; I64057; I64057.
DR RefSeq; NP_438423.1; NC_000907.1.
DR RefSeq; WP_005694049.1; NC_000907.1.
DR AlphaFoldDB; P44411; -.
DR SMR; P44411; -.
DR STRING; 71421.HI_0254; -.
DR EnsemblBacteria; AAC21920; AAC21920; HI_0254.
DR KEGG; hin:HI_0254; -.
DR PATRIC; fig|71421.8.peg.269; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_042529_14_1_6; -.
DR OMA; RVVVYFY; -.
DR PhylomeDB; P44411; -.
DR BioCyc; HINF71421:G1GJ1-268-MON; -.
DR Proteomes; UP000000579; 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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..155
FT /note="Putative peroxiredoxin bcp"
FT /id="PRO_0000135137"
FT DOMAIN 4..155
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
FT DISULFID 46..51
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
SQ SEQUENCE 155 AA; 17553 MW; 0E7AC12651107EA2 CRC64;
MNPLSVGNQA PAFTLLNQQE KFVSLSDFRG KKVLIYFYPK ALTPGCTTQA CGLRDSKSEL
DVLGLVVLGI SPDAPKKLAQ FIEKKELNFT LLSDPDHQVA EQFGVWGEKK FMGRTYDGIH
RISFLINESG TIMQVFDKFK IKDHHQMIID YLRSL
