UniProtKB - Q83CY8 (BCP_COXBU)
Protein
Putative peroxiredoxin bcp
Gene
bcp
Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Functioni
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.By similarity
Miscellaneous
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.By similarity
Catalytic activityi
- EC:1.11.1.24By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 45 | Cysteine sulfenic acid (-SOH) intermediateBy similarity | 1 |
GO - Molecular functioni
- thioredoxin peroxidase activity Source: GO_Central
GO - Biological processi
- cell redox homeostasis Source: GO_Central
- cellular response to oxidative stress Source: GO_Central
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Protein family/group databases
PeroxiBasei | 4369, CbuBCP |
Names & Taxonomyi
Protein namesi | Recommended name: Putative peroxiredoxin bcp (EC:1.11.1.24By similarity)Alternative name(s): Bacterioferritin comigratory protein Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin BcpCurated |
Gene namesi | Name:bcp Ordered Locus Names:CBU_0963 |
Organismi | Coxiella burnetii (strain RSA 493 / Nine Mile phase I) |
Taxonomic identifieri | 227377 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › |
Proteomesi |
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PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000320581 | 1 – 151 | Putative peroxiredoxin bcpAdd BLAST | 151 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 45 ↔ 50 | Redox-activeBy similarity |
Keywords - PTMi
Disulfide bondExpressioni
Developmental stagei
More than twofold more abundant in the large cell variant (LCV) stage than in the small cell variant (SCV) stage (at protein level). LCVs are more metabolically active than SCVs.1 Publication
Interactioni
Subunit structurei
Monomer.
By similarityProtein-protein interaction databases
STRINGi | 227377.CBU_0963 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 3 – 151 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | 149 |
Sequence similaritiesi
Keywords - Domaini
Redox-active centerPhylogenomic databases
eggNOGi | COG1225, Bacteria |
HOGENOMi | CLU_042529_14_1_6 |
OMAi | DSYGEKN |
Family and domain databases
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
i Sequence
Sequence statusi: Complete.
Q83CY8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSIEVGQKAP IFTLPTDEGE MLSLDDLKGK KVILYFYPKD DTPGCTKEAC
60 70 80 90 100
GFRDVWSQLS KAGVVVLGIS KDSVKAHQSF KQKYNLPFTL LSDKDNTVCE
110 120 130 140 150
QYGVMVDKNR FGKKYKGIER TTFLIDEEGV ISAVWPKVKV DGHVAEVVGR
L
Sequence cautioni
The sequence AAO90485 differs from that shown. Reason: Erroneous initiation.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE016828 Genomic DNA Translation: AAO90485.2 Different initiation. |
RefSeqi | NP_819971.2, NC_002971.3 |
Genome annotation databases
EnsemblBacteriai | AAO90485; AAO90485; CBU_0963 |
GeneIDi | 1208858 |
KEGGi | cbu:CBU_0963 |
PATRICi | fig|227377.7.peg.959 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE016828 Genomic DNA Translation: AAO90485.2 Different initiation. |
RefSeqi | NP_819971.2, NC_002971.3 |
3D structure databases
SMRi | Q83CY8 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 227377.CBU_0963 |
Protein family/group databases
PeroxiBasei | 4369, CbuBCP |
Genome annotation databases
EnsemblBacteriai | AAO90485; AAO90485; CBU_0963 |
GeneIDi | 1208858 |
KEGGi | cbu:CBU_0963 |
PATRICi | fig|227377.7.peg.959 |
Phylogenomic databases
eggNOGi | COG1225, Bacteria |
HOGENOMi | CLU_042529_14_1_6 |
OMAi | DSYGEKN |
Family and domain databases
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BCP_COXBU | |
Accessioni | Q83CY8Primary (citable) accession number: Q83CY8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 26, 2008 |
Last sequence update: | June 1, 2003 | |
Last modified: | December 2, 2020 | |
This is version 114 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families