DPS_CAMJE
ID DPS_CAMJE Reviewed; 149 AA.
AC Q0P891;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; OrderedLocusNames=Cj1534c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, IRON BINDING,
RP AND FUNCTION IN PROTECTION OF DNA FROM HYDROGEN PEROXIDE STRESS.
RX PubMed=12533477; DOI=10.1128/jb.185.3.1010-1017.2003;
RA Ishikawa T., Mizunoe Y., Kawabata S., Takade A., Harada M., Wai S.N.,
RA Yoshida S.;
RT "The iron-binding protein Dps confers hydrogen peroxide stress resistance
RT to Campylobacter jejuni.";
RL J. Bacteriol. 185:1010-1017(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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
CC (Probable). Does not bind DNA. {ECO:0000269|PubMed:12533477,
CC ECO:0000305}.
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 -!- INDUCTION: Constitutively expressed. Not induced by hydrogen peroxide
CC or by iron.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35634.1; -; Genomic_DNA.
DR PIR; D81300; D81300.
DR RefSeq; WP_002851546.1; NC_002163.1.
DR RefSeq; YP_002344906.1; NC_002163.1.
DR PDB; 3KWO; X-ray; 1.98 A; A/B/C/D=1-149.
DR PDBsum; 3KWO; -.
DR AlphaFoldDB; Q0P891; -.
DR SMR; Q0P891; -.
DR IntAct; Q0P891; 37.
DR STRING; 192222.Cj1534c; -.
DR PaxDb; Q0P891; -.
DR PRIDE; Q0P891; -.
DR EnsemblBacteria; CAL35634; CAL35634; Cj1534c.
DR GeneID; 905816; -.
DR KEGG; cje:Cj1534c; -.
DR PATRIC; fig|192222.6.peg.1511; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_2_2_7; -.
DR OMA; NTQLSNW; -.
DR BRENDA; 1.16.3.2; 13746.
DR EvolutionaryTrace; Q0P891; -.
DR Proteomes; UP000000799; Chromosome.
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 GO; GO:0042262; P:DNA protection; IDA:CACAO.
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 PIRSF; PIRSF005900; Dps; 1.
DR PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Iron; Iron storage;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..149
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253339"
FT BINDING 25
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 52
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 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:0000250"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 3..27
FT /evidence="ECO:0007829|PDB:3KWO"
FT HELIX 33..60
FT /evidence="ECO:0007829|PDB:3KWO"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3KWO"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:3KWO"
FT HELIX 119..143
FT /evidence="ECO:0007829|PDB:3KWO"
SQ SEQUENCE 149 AA; 17205 MW; 203EB8DE513D0884 CRC64;
MSVTKQLLQM QADAHHLWVK FHNYHWNVKG LQFFSIHEYT EKAYEEMAEL FDSCAERVLQ
LGEKAITCQK VLMENAKSPK VAKDCFTPLE VIELIKQDYE YLLAEFKKLN EAAEKESDTT
TAAFAQENIA KYEKSLWMIG ATLQGACKM
