BCP_XANCP
ID BCP_XANCP Reviewed; 160 AA.
AC Q8P9V9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Peroxiredoxin Bcp;
DE EC=1.11.1.24 {ECO:0000269|PubMed:19477183, ECO:0000269|PubMed:27594682};
DE AltName: Full=Bacterioferritin comigratory protein;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000305};
GN Name=bcp; OrderedLocusNames=XCC1738;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2] {ECO:0007744|PDB:3GKK, ECO:0007744|PDB:3GKM, ECO:0007744|PDB:3GKN}
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS), DISULFIDE BOND, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF CYS-48 AND CYS-84.
RX PubMed=19477183; DOI=10.1016/j.jmb.2009.05.030;
RA Liao S.J., Yang C.Y., Chin K.H., Wang A.H., Chou S.H.;
RT "Insights into the alkyl peroxide reduction pathway of Xanthomonas
RT campestris bacterioferritin comigratory protein from the trapped
RT intermediate-ligand complex structures.";
RL J. Mol. Biol. 390:951-966(2009).
RN [3] {ECO:0007744|PDB:5IM9, ECO:0007744|PDB:5IMA, ECO:0007744|PDB:5IMC}
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 2-160, DISULFIDE BOND, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27594682; DOI=10.1016/j.str.2016.07.012;
RA Perkins A., Parsonage D., Nelson K.J., Ogba O.M., Cheong P.H., Poole L.B.,
RA Karplus P.A.;
RT "Peroxiredoxin catalysis at atomic resolution.";
RL Structure 24:1668-1678(2016).
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:19477183}.
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:19477183, ECO:0000269|PubMed:27594682};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=786 uM for H(2)O(2) {ECO:0000269|PubMed:27594682};
CC KM=1840 uM for cumene hydroperoxide {ECO:0000269|PubMed:27594682};
CC KM=293 uM for TrxA (using H(2)O(2) as substrate)
CC {ECO:0000269|PubMed:27594682};
CC KM=414 uM for TrxA (using cumene hydroperoxide as substrate)
CC {ECO:0000269|PubMed:27594682};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19477183}.
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:19477183}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AE008922; AAM41029.1; -; Genomic_DNA.
DR RefSeq; NP_637105.1; NC_003902.1.
DR RefSeq; WP_011036912.1; NC_003902.1.
DR PDB; 3GKK; X-ray; 1.83 A; A=1-160.
DR PDB; 3GKM; X-ray; 1.53 A; A=1-160.
DR PDB; 3GKN; X-ray; 1.47 A; A/B=1-160.
DR PDB; 5IM9; X-ray; 1.10 A; A=2-160.
DR PDB; 5IMA; X-ray; 1.04 A; A=2-160.
DR PDB; 5IMC; X-ray; 1.05 A; A=2-160.
DR PDB; 5IMD; X-ray; 1.16 A; A=2-160.
DR PDB; 5IMF; X-ray; 1.04 A; A=2-160.
DR PDB; 5IMV; X-ray; 1.05 A; A=2-160.
DR PDB; 5IMZ; X-ray; 1.10 A; A=2-160.
DR PDB; 5INY; X-ray; 1.04 A; A=2-160.
DR PDB; 5IO0; X-ray; 1.30 A; A=2-160.
DR PDB; 5IO2; X-ray; 1.20 A; A=2-160.
DR PDB; 5IOW; X-ray; 1.35 A; A=2-160.
DR PDB; 5IOX; X-ray; 1.30 A; A=1-160.
DR PDB; 5IPG; X-ray; 1.35 A; A=1-160.
DR PDB; 5IPH; X-ray; 1.30 A; A=2-160.
DR PDBsum; 3GKK; -.
DR PDBsum; 3GKM; -.
DR PDBsum; 3GKN; -.
DR PDBsum; 5IM9; -.
DR PDBsum; 5IMA; -.
DR PDBsum; 5IMC; -.
DR PDBsum; 5IMD; -.
DR PDBsum; 5IMF; -.
DR PDBsum; 5IMV; -.
DR PDBsum; 5IMZ; -.
DR PDBsum; 5INY; -.
DR PDBsum; 5IO0; -.
DR PDBsum; 5IO2; -.
DR PDBsum; 5IOW; -.
DR PDBsum; 5IOX; -.
DR PDBsum; 5IPG; -.
DR PDBsum; 5IPH; -.
DR AlphaFoldDB; Q8P9V9; -.
DR SMR; Q8P9V9; -.
DR STRING; 340.xcc-b100_2523; -.
DR DrugBank; DB04640; Naphthalene-2,6-disulfonic acid.
DR EnsemblBacteria; AAM41029; AAM41029; XCC1738.
DR KEGG; xcc:XCC1738; -.
DR PATRIC; fig|190485.4.peg.1853; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_042529_14_1_6; -.
DR OMA; RVVVYFY; -.
DR EvolutionaryTrace; Q8P9V9; -.
DR Proteomes; UP000001010; 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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..160
FT /note="Peroxiredoxin Bcp"
FT /id="PRO_0000441071"
FT DOMAIN 4..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:19477183,
FT ECO:0000305|PubMed:27594682"
FT DISULFID 48..84
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:19477183,
FT ECO:0000269|PubMed:27594682, ECO:0007744|PDB:3GKK,
FT ECO:0007744|PDB:5IOX"
FT MUTAGEN 48
FT /note="C->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19477183"
FT MUTAGEN 84
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19477183"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5IMA"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5IMA"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:5IMA"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:5IMA"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5IMA"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5IMA"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:5IMA"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:5IMA"
SQ SEQUENCE 160 AA; 17278 MW; 7DC8B47B3D7442CF CRC64;
MTDAVLELPA ATFDLPLSLS GGTQTTLRAH AGHWLVIYFY PKDSTPGCTT EGLDFNALLP
EFDKAGAKIL GVSRDSVKSH DNFCAKQGFA FPLVSDGDEA LCRAFDVIKE KNMYGKQVLG
IERSTFLLSP EGQVVQAWRK VKVAGHADAV LAALKAHAKQ
