DPS_BREBE
ID DPS_BREBE Reviewed; 149 AA.
AC P83695;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps;
OS Brevibacillus brevis (Bacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1393;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON, AND SUBUNIT.
RX PubMed=12767829; DOI=10.1016/s0022-2836(03)00466-2;
RA Ren B., Tibbelin G., Kajino T., Asami O., Ladenstein R.;
RT "The multi-layered structure of Dps with a novel di-nuclear ferroxidase
RT center.";
RL J. Mol. Biol. 329:467-477(2003).
CC -!- FUNCTION: During stationary phase, binds the chromosome non-
CC specifically, forming a highly ordered and stable dps-DNA co-crystal
CC within which chromosomal DNA is condensed and protected from diverse
CC damages. It 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: 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:12767829}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {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 PDB; 1N1Q; X-ray; 2.20 A; A/B/C/D=1-149.
DR PDBsum; 1N1Q; -.
DR AlphaFoldDB; P83695; -.
DR SMR; P83695; -.
DR EvolutionaryTrace; P83695; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 GO; GO:0030261; P:chromosome condensation; 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; DNA condensation; DNA-binding; Iron; Iron storage;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..149
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253330"
FT BINDING 31
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:12767829"
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:12767829"
FT BINDING 62
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:12767829"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:12767829"
FT HELIX 4..33
FT /evidence="ECO:0007829|PDB:1N1Q"
FT HELIX 39..66
FT /evidence="ECO:0007829|PDB:1N1Q"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:1N1Q"
FT HELIX 93..120
FT /evidence="ECO:0007829|PDB:1N1Q"
FT HELIX 124..148
FT /evidence="ECO:0007829|PDB:1N1Q"
SQ SEQUENCE 149 AA; 16329 MW; 2EAD673DB32502BE CRC64;
MKTSIQQLVA VLLNRQVANW VVLYVKLHNF HWNVNGPNFF TLHEKFEELY TEASGHIDTL
AERVLSIGGS PIATLAASLE EASIKEATGG ESAAEMVSSV VNDFVDLVGE LKVARDVADE
ADDEATADML DAIEAGLEKH VWMLEAFLE
