DPS_KLEP3
ID DPS_KLEP3 Reviewed; 167 AA.
AC B5XYT2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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}; OrderedLocusNames=KPK_3728;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI08129.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XYT2; -.
DR SMR; B5XYT2; -.
DR EnsemblBacteria; ACI08129; ACI08129; KPK_3728.
DR KEGG; kpe:KPK_3728; -.
DR HOGENOM; CLU_098183_1_2_6; -.
DR OMA; DDYSIGR; -.
DR OrthoDB; 1742631at2; -.
DR Proteomes; UP000001734; 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.
FT CHAIN 1..167
FT /note="DNA protection during starvation protein"
FT /id="PRO_1000145908"
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
