UniProt Accession

 DPS_ECOLI; P0ABT2; P27430 

Genbank Protein ID

 X69337; U04242; U00096; AP009048; X14180 

Genbank Nucleotide ID

 CAA49169.1; AAA21855.1; AAC73899.1; BAA35484.1 

Protein Name

 DNA protection during starvation protein 

Protein Synonyms/Alias

  

Gene Name

 dps 

Gene Synonyms/Alias

 pexB; vtm; b0812; JW0797 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
5	***MSTAKLVKSKAT	acetylation	[1]
8	MSTAKLVKSKATNLL	acetylation	[1]
10	TAKLVKSKATNLLYT	acetylation	[1]
26	NDVSDSEKKATVELL	acetylation	[1]
27	DVSDSEKKATVELLN	acetylation	[1]
101	TTQVINSKTPLKSYP	acetylation	[1, 2]
105	INSKTPLKSYPLDIH	acetylation	[1, 2]
105	INSKTPLKSYPLDIH	pupylation	[3]
119	HNVQDHLKELADRYA	acetylation	[1, 2]
134	IVANDVRKAIGEAKD	acetylation	[1]
140	RKAIGEAKDDDTADI	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [3] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222] 

Functional Description

 During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co- crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Dps also protects the cell from UV and gamma irradiation, iron and copper toxicity, thermal stress and acid and base shocks. Also shows a weak catalase activity. 

Sequence Annotation

 METAL 51 51 Iron 1; shared with dodecameric partner.
 METAL 78 78 Iron 1.
 METAL 82 82 Iron 1.
 METAL 82 82 Iron 2 (Probable).  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; DNA condensation; DNA-binding; Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 167 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:HAMAP.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IDA:EcoCyc.
 GO:0008199; F:ferric iron binding; IEA:HAMAP.
 GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IEA:InterPro.
 GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
 GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
 GO:0042594; P:response to starvation; IDA:EcoCyc. 

Interpro

 IPR002177; DPS_DNA-bd.
 IPR023188; DPS_DNA-bd_CS.
 IPR023067; Dps_gammaproteobac.
 IPR009078; Ferritin-like_SF.
 IPR012347; Ferritin-rel.
 IPR008331; Ferritin_DPS_dom. 

Pfam

 PF00210; Ferritin 

SMART

  

PROSITE

 PS00818; DPS_1
 PS00819; DPS_2 

PRINTS

 PR01346; HELNAPAPROT.