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Protein

DNA protection during starvation protein

Gene

dps

Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
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. Does not bind DNA.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31Iron 1; shared with dodecameric partner1 Publication1
Metal bindingi58Iron 11 Publication1
Metal bindingi62Iron 11 Publication1
Metal bindingi62Iron 21 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.16.3.1. 3044.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA protection during starvation protein (EC:1.16.-.-)
Alternative name(s):
Ferritin-like protein
Non-heme iron-containing ferritin
Gene namesi
Name:dps
Synonyms:flp, fri
Ordered Locus Names:lin0942
OrganismiListeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Taxonomic identifieri272626 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000002513 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31H → G: Slight decrease in DNA protection and significant decrease in iron affinity. Retains only one third of wild-type DNA protection and loses iron binding ability; when associated with G-43. 1 Publication1
Mutagenesisi43H → G: Slight decrease in DNA protection and significant decrease iron affinity. Retains only one third of wild-type DNA protection and loses iron-binding ability; when associated with G-31. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002016571 – 156DNA protection during starvation proteinAdd BLAST156

Expressioni

Inductioni

By iron limitation and stationary growth phase.1 Publication

Interactioni

Subunit structurei

Homododecamer. The 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe3+ can be deposited.1 Publication

Protein-protein interaction databases

STRINGi272626.lin0942.

Structurei

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 33Combined sources25
Helixi39 – 66Combined sources28
Helixi75 – 81Combined sources7
Helixi95 – 123Combined sources29
Helixi126 – 149Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QGHX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L1-156[»]
2BJYX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-156[»]
2BK6X-ray2.19A/B/C/D/E/F1-156[»]
2BKCX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y1-156[»]
ProteinModelPortaliP80725.
SMRiP80725.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80725.

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

eggNOGiENOG4105HUF. Bacteria.
COG0783. LUCA.
HOGENOMiHOG000273542.
KOiK04047.
OMAiVGPQFRS.
OrthoDBiPOG091H00MO.

Family and domain databases

CDDicd01043. DPS. 1 hit.
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.
PS00819. DPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80725-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTINSVDTK EFLNHQVANL NVFTVKIHQI HWYMRGHNFF TLHEKMDDLY
60 70 80 90 100
SEFGEQMDEV AERLLAIGGS PFSTLKEFLE NASVEEAPYT KPKTMDQLME
110 120 130 140 150
DLVGTLELLR DEYKQGIELT DKEGDDVTND MLIAFKASID KHIWMFKAFL

GKAPLE
Length:156
Mass (Da):18,049
Last modified:November 1, 1997 - v1
Checksum:i5FC9FFF5EE7FB6F8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63R → L (PubMed:12383509).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ244014 Genomic DNA. Translation: CAB65175.2.
AL596167 Genomic DNA. Translation: CAC96173.1.
PIRiAE1550.
RefSeqiWP_003761404.1. NC_003212.1.

Genome annotation databases

EnsemblBacteriaiCAC96173; CAC96173; CAC96173.
KEGGilin:fri.
PATRICi20298599. VBILisInn102668_0967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ244014 Genomic DNA. Translation: CAB65175.2.
AL596167 Genomic DNA. Translation: CAC96173.1.
PIRiAE1550.
RefSeqiWP_003761404.1. NC_003212.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QGHX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L1-156[»]
2BJYX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-156[»]
2BK6X-ray2.19A/B/C/D/E/F1-156[»]
2BKCX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y1-156[»]
ProteinModelPortaliP80725.
SMRiP80725.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272626.lin0942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC96173; CAC96173; CAC96173.
KEGGilin:fri.
PATRICi20298599. VBILisInn102668_0967.

Phylogenomic databases

eggNOGiENOG4105HUF. Bacteria.
COG0783. LUCA.
HOGENOMiHOG000273542.
KOiK04047.
OMAiVGPQFRS.
OrthoDBiPOG091H00MO.

Enzyme and pathway databases

BRENDAi1.16.3.1. 3044.

Miscellaneous databases

EvolutionaryTraceiP80725.

Family and domain databases

CDDicd01043. DPS. 1 hit.
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.
PS00819. DPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPS_LISIN
AccessioniPrimary (citable) accession number: P80725
Secondary accession number(s): Q9RE06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

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.