DPS2_DEIRA
ID DPS2_DEIRA Reviewed; 241 AA.
AC Q9RZN1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA protection during starvation protein 2;
DE EC=1.16.-.-;
GN Name=dps2; Synonyms=dps-2; OrderedLocusNames=DR_B0092;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OG Plasmid megaplasmid MP1.
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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). {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 subunits form a hollow sphere into which
CC the mineral iron core of up to 500 Fe(3+) can be deposited (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AE001826; AAF12541.1; -; Genomic_DNA.
DR PIR; B75628; B75628.
DR RefSeq; NP_051625.1; NC_000958.1.
DR RefSeq; WP_010883959.1; NZ_CP015083.1.
DR PDB; 2C2J; X-ray; 2.05 A; A=31-241.
DR PDB; 2C6R; X-ray; 2.10 A; A=31-241.
DR PDB; 6TB5; X-ray; 1.83 A; A=31-241.
DR PDB; 6TGT; X-ray; 2.15 A; A=31-239.
DR PDBsum; 2C2J; -.
DR PDBsum; 2C6R; -.
DR PDBsum; 6TB5; -.
DR PDBsum; 6TGT; -.
DR AlphaFoldDB; Q9RZN1; -.
DR SASBDB; Q9RZN1; -.
DR SMR; Q9RZN1; -.
DR EnsemblBacteria; AAF12541; AAF12541; DR_B0092.
DR KEGG; dra:DR_B0092; -.
DR PATRIC; fig|243230.17.peg.90; -.
DR HOGENOM; CLU_090981_0_0_0; -.
DR InParanoid; Q9RZN1; -.
DR OMA; WFLFAHI; -.
DR OrthoDB; 1129656at2; -.
DR EvolutionaryTrace; Q9RZN1; -.
DR Proteomes; UP000002524; Plasmid megaplasmid MP1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
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 PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW Plasmid; Reference proteome.
FT CHAIN 1..241
FT /note="DNA protection during starvation protein 2"
FT /id="PRO_0000253328"
FT REGION 25..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two dodecameric
FT partners"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two dodecameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two dodecameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 73..102
FT /evidence="ECO:0007829|PDB:6TB5"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6TB5"
FT HELIX 108..135
FT /evidence="ECO:0007829|PDB:6TB5"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:6TB5"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6TB5"
FT HELIX 163..188
FT /evidence="ECO:0007829|PDB:6TB5"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6TB5"
FT HELIX 193..214
FT /evidence="ECO:0007829|PDB:6TB5"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6TB5"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6TB5"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6TB5"
SQ SEQUENCE 241 AA; 26089 MW; 18FFC6F5D629EE75 CRC64;
MRHSVKTVVV VSSLLLGTAL AGGAGAQSAG NGVPSTNVNT PAPNTGQSTA QNTNTASPLP
YNRATTLPAA GTEDLKKSVQ ALQNTLTELQ ALQLQTKQAH WNVSGTLWYT LHELLQDHYE
GISKFADDVA ERQLSVGASS DGRAITIVAA SRLPEIPGGF LDDAQVIQFF TYQYETVGQR
IHQRVGDVEK VDPTTANLLQ EVEHIIEKYQ WQMRAFLQNT PTDPNTGFDI NNGKPVPLRG
R
