Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA protection during starvation protein

Gene

dps

Organism
Mycobacterium smegmatis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). It protects DNA from hydroxyl radical-mediated cleavage. Binds DNA with no apparent sequence specificity without self-aggregation nor promotion of DNA condensation. Is unable to protect DNA from DNase-mediated cleavage.By similarity1 Publication

Catalytic activityi

2 Fe2+ + H2O2 + 2 H+ = 2 Fe3+ + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Iron 1; shared with dodecameric partner2 Publications
Metal bindingi66 – 661Iron 12 Publications
Metal bindingi70 – 701Iron 12 Publications
Metal bindingi70 – 701Iron 22 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

DNA-binding, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA protection during starvation protein (EC:1.16.-.-)
Gene namesi
Name:dps
OrganismiMycobacterium smegmatis
Taxonomic identifieri1772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183DNA protection during starvation proteinPRO_0000253333Add
BLAST

Interactioni

Subunit structurei

The 12 identical subunits form a hollow sphere into which the mineral iron core of up to 500 Fe3+ can be deposited (By similarity). Homododecamer.By similarity3 Publications

Protein-protein interaction databases

STRINGi246196.MSMEG_6467.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 4128Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 7428Combined sources
Helixi83 – 897Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 12726Combined sources
Turni128 – 1303Combined sources
Helixi132 – 15625Combined sources
Beta strandi159 – 1613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UVHX-ray2.80A/B/C/D1-183[»]
1VEIX-ray2.85A1-183[»]
1VELX-ray2.99A/B/C/D/E/F1-183[»]
1VEQX-ray3.98A/B/C/D/E/F/G/H/I/J/K/L1-183[»]
2YW6X-ray2.53A/B/C1-183[»]
2YW7X-ray3.30A/B/C/D/E/F/G/H/I/J1-183[»]
ProteinModelPortaliP0C558.
SMRiP0C558. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C558.

Family & Domainsi

Domaini

12 di-nuclear ferroxidase centers are located at the interfaces between subunits related by 2-fold symmetry axes.

Sequence similaritiesi

Belongs to the Dps family.Curated

Phylogenomic databases

eggNOGiENOG4105DPV. Bacteria.
COG0783. LUCA.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002177. DPS_DNA-bd.
IPR023188. DPS_DNA-bd_CS.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF005900. Dps. 1 hit.
PRINTSiPR01346. HELNAPAPROT.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00818. DPS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C558-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSFTIPGLS DKKASDVADL LQKQLSTYND LHLTLKHVHW NVVGPNFIGV
60 70 80 90 100
HEMIDPQVEL VRGYADEVAE RIATLGKSPK GTPGAIIKDR TWDDYSVERD
110 120 130 140 150
TVQAHLAALD LVYNGVIEDT RKSIEKLEDL DLVSQDLLIA HAGELEKFQW
160 170 180
FVRAHLESAG GQLTHEGQST EKGAADKARR KSA
Length:183
Mass (Da):20,270
Last modified:July 10, 2007 - v1
Checksum:i3ACB34B43B23F877
GO

Sequence databases

RefSeqiWP_003897878.1. NZ_LN831039.1.

Cross-referencesi

Sequence databases

RefSeqiWP_003897878.1. NZ_LN831039.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UVHX-ray2.80A/B/C/D1-183[»]
1VEIX-ray2.85A1-183[»]
1VELX-ray2.99A/B/C/D/E/F1-183[»]
1VEQX-ray3.98A/B/C/D/E/F/G/H/I/J/K/L1-183[»]
2YW6X-ray2.53A/B/C1-183[»]
2YW7X-ray3.30A/B/C/D/E/F/G/H/I/J1-183[»]
ProteinModelPortaliP0C558.
SMRiP0C558. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_6467.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DPV. Bacteria.
COG0783. LUCA.

Miscellaneous databases

EvolutionaryTraceiP0C558.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002177. DPS_DNA-bd.
IPR023188. DPS_DNA-bd_CS.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF005900. Dps. 1 hit.
PRINTSiPR01346. HELNAPAPROT.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00818. DPS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPS_MYCSM
AccessioniPrimary (citable) accession number: P0C558
Secondary accession number(s): Q8VP75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: March 16, 2016
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1UVH.Curated

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.