DPS2_BACAN
ID DPS2_BACAN Reviewed; 146 AA.
AC Q8RPQ2; Q6HR83; Q6KKJ8; Q81XE7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA protection during starvation protein 2;
DE EC=1.16.-.-;
GN Name=dps2; Synonyms=dlp1; OrderedLocusNames=BA_5290, GBAA_5290, BAS4914;
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 (2.5 ANGSTROMS) OF
RP 4-145 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 reaction (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; AF374268; AAM18635.1; -; Genomic_DNA.
DR EMBL; AE016879; AAP28955.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34421.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57205.1; -; Genomic_DNA.
DR RefSeq; NP_847469.1; NC_003997.3.
DR RefSeq; WP_001041890.1; NZ_WXXJ01000014.1.
DR RefSeq; YP_031155.1; NC_005945.1.
DR PDB; 1JI5; X-ray; 2.50 A; A/B/C/D=4-145.
DR PDBsum; 1JI5; -.
DR AlphaFoldDB; Q8RPQ2; -.
DR SMR; Q8RPQ2; -.
DR STRING; 260799.BAS4914; -.
DR DNASU; 1084783; -.
DR EnsemblBacteria; AAP28955; AAP28955; BA_5290.
DR EnsemblBacteria; AAT34421; AAT34421; GBAA_5290.
DR GeneID; 45024903; -.
DR GeneID; 64204048; -.
DR KEGG; ban:BA_5290; -.
DR KEGG; bar:GBAA_5290; -.
DR KEGG; bat:BAS4914; -.
DR PATRIC; fig|198094.11.peg.5251; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_2_2_9; -.
DR OMA; DDYSIGR; -.
DR EvolutionaryTrace; Q8RPQ2; -.
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.
DR PROSITE; PS00819; DPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..146
FT /note="DNA protection during starvation protein 2"
FT /id="PRO_0000253327"
FT BINDING 27
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 54
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 58
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 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:11836250"
FT HELIX 5..29
FT /evidence="ECO:0007829|PDB:1JI5"
FT HELIX 35..62
FT /evidence="ECO:0007829|PDB:1JI5"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1JI5"
FT HELIX 89..116
FT /evidence="ECO:0007829|PDB:1JI5"
FT HELIX 120..144
FT /evidence="ECO:0007829|PDB:1JI5"
SQ SEQUENCE 146 AA; 16910 MW; A2CAD49BA33B76E0 CRC64;
MNKQVIEVLN KQVADWSVLF TKLHNFHWYV KGPQFFTLHE KFEELYTESA THIDEIAERI
LAIGGKPVAT MKEYLEISSI QEAAYGETAE GMVEAIMKDY EMMLVELKKG MEIAQNSDDE
MTSDLLLGIY TELEKHAWML RAFLNQ
