DPS1_BACAN
ID DPS1_BACAN Reviewed; 147 AA.
AC Q8RPQ1; Q6HZV3; Q6KTT5; Q81RM9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=DNA protection during starvation protein 1;
DE EC=1.16.-.-;
GN Name=dps1; Synonyms=dlp2; OrderedLocusNames=BA_2013, GBAA_2013, BAS1871;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS)
RP OF 2-147 IN COMPLEX WITH IRON, AND SUBUNIT.
RC STRAIN=9131;
RX PubMed=11836250; DOI=10.1074/jbc.m112378200;
RA Papinutto E., Dundon W.G., Pitulis N., Battistutta R., Montecucco C.,
RA Zanotti G.;
RT "Structure of two iron-binding proteins from Bacillus anthracis.";
RL J. Biol. Chem. 277:15093-15098(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 Fe(2+) ion (By
CC similarity). It is capable of binding and sequestering Fe(2+) ion. Does
CC not bind DNA. {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: The 12 subunits form a hollow sphere into which the mineral
CC iron core of up to 500 Fe(3+) can be deposited (By similarity).
CC Homododecamer. {ECO:0000250, ECO:0000269|PubMed:11836250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the interfaces
CC between subunits related by 2-fold symmetry axes.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AF374269; AAM18636.1; -; Genomic_DNA.
DR EMBL; AE016879; AAP25903.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT31135.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT54186.1; -; Genomic_DNA.
DR RefSeq; NP_844417.1; NC_003997.3.
DR RefSeq; WP_000105197.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_028135.1; NC_005945.1.
DR PDB; 1JIG; X-ray; 1.46 A; A/B/C/D=2-147.
DR PDBsum; 1JIG; -.
DR AlphaFoldDB; Q8RPQ1; -.
DR SMR; Q8RPQ1; -.
DR STRING; 260799.BAS1871; -.
DR DNASU; 1085881; -.
DR EnsemblBacteria; AAP25903; AAP25903; BA_2013.
DR EnsemblBacteria; AAT31135; AAT31135; GBAA_2013.
DR GeneID; 45021934; -.
DR KEGG; ban:BA_2013; -.
DR KEGG; bar:GBAA_2013; -.
DR KEGG; bat:BAS1871; -.
DR PATRIC; fig|198094.11.peg.1988; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_2_2_9; -.
DR OMA; LYLQTHN; -.
DR EvolutionaryTrace; Q8RPQ1; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
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 PIRSF; PIRSF005900; Dps; 1.
DR PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00818; DPS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..147
FT /note="DNA protection during starvation protein 1"
FT /id="PRO_0000253325"
FT BINDING 29
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:0000269|PubMed:11836250"
FT BINDING 56
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:0000269|PubMed:11836250"
FT BINDING 60
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:0000269|PubMed:11836250"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:11836250"
FT HELIX 4..31
FT /evidence="ECO:0007829|PDB:1JIG"
FT HELIX 37..64
FT /evidence="ECO:0007829|PDB:1JIG"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:1JIG"
FT HELIX 91..118
FT /evidence="ECO:0007829|PDB:1JIG"
FT HELIX 122..145
FT /evidence="ECO:0007829|PDB:1JIG"
SQ SEQUENCE 147 AA; 16649 MW; 2741651884FCCCCD CRC64;
MSTKTNVVEV LNKQVANWNV LYVKLHNYHW YVTGPHFFTL HEKFEEFYNE AGTYIDELAE
RILALEGKPL ATMKEYLATS SVNEGTSKES AEEMVQTLVN DYSALIQELK EGMEVAGEAG
DATSADMLLA IHTTLEQHVW MLSAFLK
