DPS_STRMG
ID DPS_STRMG Reviewed; 175 AA.
AC Q9KWH3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; ORFNames=dpr/ORF 1;
OS Streptococcus mutans.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1309;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC STRAIN=GS-5;
RX PubMed=10879495; DOI=10.1271/bbb.64.1106;
RA Yamamoto Y., Higuchi M., Poole L.B., Kamio Y.;
RT "Identification of a new gene responsible for the oxygen tolerance in
RT aerobic life of Streptococcus mutans.";
RL Biosci. Biotechnol. Biochem. 64:1106-1109(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15, AND INDUCTION.
RC STRAIN=GS-5;
RX PubMed=10850989; DOI=10.1128/jb.182.13.3740-3747.2000;
RA Yamamoto Y., Higuchi M., Poole L.B., Kamio Y.;
RT "Role of the dpr product in oxygen tolerance in Streptococcus mutans.";
RL J. Bacteriol. 182:3740-3747(2000).
RN [3]
RP FUNCTION IN PREVENTION OF HYDROXYL RADICAL FORMATION, AND SUBUNIT.
RC STRAIN=GS-5;
RX PubMed=12003933; DOI=10.1128/jb.184.11.2931-2939.2002;
RA Yamamoto Y., Poole L.B., Hantgan R.R., Kamio Y.;
RT "An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-
RT dependent hydroxyl radical formation in vitro.";
RL J. Bacteriol. 184:2931-2939(2002).
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 (By similarity). It binds and incorporates Fe(2+)
CC ion. Effectively inhibits hydroxyl radical formation by the Fenton
CC reaction and is essential for colony formation in the presence of air.
CC Is also able to bind zinc ion. Does not bind DNA. {ECO:0000250,
CC ECO:0000269|PubMed:12003933}.
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 (Probable). The oligomer forms a hollow sphere
CC and can store up to 480 Fe(3+). {ECO:0000269|PubMed:12003933,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Induced by air. {ECO:0000269|PubMed:10850989}.
CC -!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the interfaces
CC between subunits related by 2-fold symmetry axes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AB036428; BAA96472.1; -; Genomic_DNA.
DR PIR; JC7274; JC7274.
DR RefSeq; WP_002264439.1; NZ_RXZB01000001.1.
DR AlphaFoldDB; Q9KWH3; -.
DR SMR; Q9KWH3; -.
DR STRING; 1198676.SMUGS5_02375; -.
DR eggNOG; COG0783; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
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 CDD; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
DR InterPro; IPR023188; DPS_DNA-bd_CS.
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.
DR PROSITE; PS00818; DPS_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10850989,
FT ECO:0000269|PubMed:10879495"
FT CHAIN 2..175
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253336"
FT BINDING 50
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 77
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 81
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 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 175 AA; 19617 MW; 0025527959B658A6 CRC64;
MTNTITENIY ASIIHQVEKK ENSGNEKTKA VLNQAVADLS KAASIVHQVH WYMRGSGFLY
LHPKMDELMD ALNGHLDEIS ERLITIGGAP FSTLKEFDEN SRLEETVGTW DKSITDHLKR
LVQVYDYLSS LYQVGLDVTD EEDDAVSNDI FTAAQTEAQK TIWMLQAELG QAPGL
