DPS_PYRFU
ID DPS_PYRFU Reviewed; 185 AA.
AC Q8U1L3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; OrderedLocusNames=PF1193;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP IRON OXIDATION, AND SUBUNIT.
RX PubMed=16412514; DOI=10.1016/j.jinorgbio.2005.12.001;
RA Ramsay B., Wiedenheft B., Allen M., Gauss G.H., Martin Lawrence C.,
RA Young M., Douglas T.;
RT "Dps-like protein from the hyperthermophilic archaeon Pyrococcus
RT furiosus.";
RL J. Inorg. Biochem. 100:1061-1068(2006).
CC -!- FUNCTION: Protects DNA from oxidative damage by sequestering
CC intracellular Fe(2+) ion and storing it in the form of Fe(3+)
CC oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions,
CC which prevents hydroxyl radical production by the Fenton reaction (By
CC similarity). It efficiently oxidizes Fe(2+) in the presence of hydrogen
CC peroxide and stores it. {ECO:0000250}.
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 -!- SUBUNIT: Homododecamer. The 12 identical subunits form a holow sphere
CC unto which the mineral iron core of up to 300 Fe(3+) can be deposited.
CC {ECO:0000269|PubMed:16412514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81317.1; -; Genomic_DNA.
DR RefSeq; WP_011012334.1; NZ_CP023154.1.
DR PDB; 7STW; EM; 2.37 A; A/B/C/D/E/F/G/H/I/J/K/L=1-185.
DR PDBsum; 7STW; -.
DR AlphaFoldDB; Q8U1L3; -.
DR SMR; Q8U1L3; -.
DR STRING; 186497.PF1193; -.
DR PRIDE; Q8U1L3; -.
DR EnsemblBacteria; AAL81317; AAL81317; PF1193.
DR GeneID; 41713001; -.
DR KEGG; pfu:PF1193; -.
DR PATRIC; fig|186497.12.peg.1254; -.
DR eggNOG; arCOG01093; Archaea.
DR HOGENOM; CLU_104506_4_0_2; -.
DR OMA; TFYYYTI; -.
DR OrthoDB; 61631at2157; -.
DR PhylomeDB; Q8U1L3; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR CDD; cd01052; DPSL; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR014490; Dps-like.
DR InterPro; IPR033921; DPSL_diiron-bd_dom.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF018063; Ferrtn_UCP018063; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..185
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253335"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT HELIX 16..42
FT /evidence="ECO:0007829|PDB:7STW"
FT HELIX 46..76
FT /evidence="ECO:0007829|PDB:7STW"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:7STW"
FT HELIX 105..130
FT /evidence="ECO:0007829|PDB:7STW"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:7STW"
FT HELIX 135..159
FT /evidence="ECO:0007829|PDB:7STW"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:7STW"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:7STW"
SQ SEQUENCE 185 AA; 21357 MW; 83611790774E8DAC CRC64;
MPEHNRRLVE RTGIDVEKLL ELLIKAAAAE FTTYYYYTIL RNHATGLEGE AIKEIIEDAR
LEDRNHFEAL VPRIYELGGE LPRDIREFAD LASCRDAYLP EEPTIENILK VLLEAERCAV
GVYTEICNYT FGKDPRTYDL ALAILHEEIE HEAWFEELLT GKPSGHFRRG KPGESPYVSK
FLKTR
