DPS_KLEP7
ID DPS_KLEP7 Reviewed; 167 AA.
AC A6T6Q6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=DNA protection during starvation protein {ECO:0000255|HAMAP-Rule:MF_01441};
DE EC=1.16.-.- {ECO:0000255|HAMAP-Rule:MF_01441};
GN Name=dps {ECO:0000255|HAMAP-Rule:MF_01441};
GN OrderedLocusNames=KPN78578_08160; ORFNames=KPN_00841;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: During stationary phase, binds the chromosome non-
CC specifically, forming a highly ordered and stable dps-DNA co-crystal
CC within which chromosomal DNA is condensed and protected from diverse
CC damages. It protects DNA from oxidative damage by sequestering
CC intracellular Fe(2+) ion and storing it in the form of Fe(3+)
CC oxyhydroxide mineral, which can be released after reduction. One
CC hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl
CC radical production by the Fenton reaction. {ECO:0000255|HAMAP-
CC Rule:MF_01441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:48712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01441};
CC -!- SUBUNIT: Homododecamer. The 12 subunits form a hollow sphere into which
CC the mineral iron core of up to 500 Fe(3+) can be deposited.
CC {ECO:0000255|HAMAP-Rule:MF_01441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01441}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000255|HAMAP-
CC Rule:MF_01441}.
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DR EMBL; CP000647; ABR76277.1; -; Genomic_DNA.
DR RefSeq; WP_002895841.1; NC_009648.1.
DR AlphaFoldDB; A6T6Q6; -.
DR SMR; A6T6Q6; -.
DR STRING; 272620.KPN_00841; -.
DR jPOST; A6T6Q6; -.
DR EnsemblBacteria; ABR76277; ABR76277; KPN_00841.
DR GeneID; 61332038; -.
DR KEGG; kpn:KPN_00841; -.
DR HOGENOM; CLU_098183_1_2_6; -.
DR OMA; DDYSIGR; -.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008199; F:ferric iron binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR CDD; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR HAMAP; MF_01441; Dps; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
DR InterPro; IPR023188; DPS_DNA-bd_CS.
DR InterPro; IPR023067; Dps_gammaproteobac.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR42932; PTHR42932; 1.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF005900; Dps; 1.
DR PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00818; DPS_1; 1.
DR PROSITE; PS00819; DPS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA condensation; DNA-binding; Iron; Iron storage;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..167
FT /note="DNA protection during starvation protein"
FT /id="PRO_1000024417"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
SQ SEQUENCE 167 AA; 18708 MW; 0949974B131D4C6E CRC64;
MSTAKLVKSK ASNLVYTRND VADSEKKATI ELLNRQVIQF IDLSLITKQA HWNMRGANFI
AVHEMLDGFR TALTEHLDTM AERAVQLGGV ALGTTQVINS KTPLQSYPLD IHHVQDHLKA
LADRYAVVAN DVRKAIDEAK DEDTADIFTA ASRDLDKFLW FIEANIE
