DPS_SACS2
ID DPS_SACS2 Reviewed; 188 AA.
AC P95855; Q9HHC3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; OrderedLocusNames=SSO2079; ORFNames=C06008;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 151-188.
RC STRAIN=ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1;
RX PubMed=12441394; DOI=10.1110/ps.0222402;
RA Cosper N.J., Eby D.M., Kounosu A., Kurosawa N., Neidle E.L.,
RA Kurtz D.M. Jr., Iwasaki T., Scott R.A.;
RT "Redox-dependent structural changes in archaeal and bacterial Rieske-type
RT [2Fe-2S] clusters.";
RL Protein Sci. 11:2969-2973(2002).
RN [4]
RP FUNCTION IN IRON OXIDATION, FUNCTION IN MINERALIZATION, AND SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=16024730; DOI=10.1073/pnas.0501497102;
RA Wiedenheft B., Mosolf J., Willits D., Yeager M., Dryden K.A., Young M.,
RA Douglas T.;
RT "An archaeal antioxidant: characterization of a Dps-like protein from
RT Sulfolobus solfataricus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10551-10556(2005).
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). In vitro, it efficiently oxidizes Fe(2+) in the presence
CC of hydrogen peroxide and stores it as a mineral core. {ECO:0000250,
CC ECO:0000269|PubMed:16024730}.
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 hollow sphere
CC into which the mineral iron core of up to 300 Fe(3+) can be deposited.
CC {ECO:0000269|PubMed:16024730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}.
CC -!- INDUCTION: Up-regulated in cultures grown in iron-depleted media and
CC upon hydrogen peroxide stress, but is not induced by other stress.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; Y08256; CAA69491.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42260.1; -; Genomic_DNA.
DR EMBL; AB047031; BAB17764.1; -; Genomic_DNA.
DR PIR; S73096; S73096.
DR RefSeq; WP_009989805.1; NC_002754.1.
DR PDB; 2CLB; X-ray; 2.40 A; A/B/C/D/M/N/O/P=1-188.
DR PDBsum; 2CLB; -.
DR AlphaFoldDB; P95855; -.
DR SMR; P95855; -.
DR STRING; 273057.SSO2079; -.
DR EnsemblBacteria; AAK42260; AAK42260; SSO2079.
DR GeneID; 44130785; -.
DR KEGG; sso:SSO2079; -.
DR PATRIC; fig|273057.12.peg.2157; -.
DR eggNOG; arCOG01093; Archaea.
DR HOGENOM; CLU_104506_4_0_2; -.
DR InParanoid; P95855; -.
DR OMA; TFYYYTI; -.
DR PhylomeDB; P95855; -.
DR EvolutionaryTrace; P95855; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
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; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..188
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253338"
FT BINDING 37
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:2CLB"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 23..49
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 60..83
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:2CLB"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 113..138
FT /evidence="ECO:0007829|PDB:2CLB"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2CLB"
FT HELIX 143..167
FT /evidence="ECO:0007829|PDB:2CLB"
SQ SEQUENCE 188 AA; 21770 MW; 617F4CA5A2316F6C CRC64;
MQEKPQEPKV VGVEILEKSG LDIKKLVDKL VKATAAEFTT YYYYTILRMH LTGMEGEGLK
EIAEDARLED RLHFELMTQR IYELGGGLPR DIRQLADISA CSDAYLPENW KDPKEILKVL
LEAEQCAIRT WKEVCDMTYG KDPRTYDLAQ RILQEEIEHE AWFLELLYGR PSGHFRRSSP
GNAPYSKK
