DPS_HALSA
ID DPS_HALSA Reviewed; 182 AA.
AC Q9HMP7;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
DE AltName: Full=Bacterioferritin DpsA;
GN Name=dps; Synonyms=dpsA; OrderedLocusNames=VNG_2443G; ORFNames=OE4427R;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Oesterhelt D., Pfeiffer F.;
RL Unpublished observations (NOV-2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP PROTEIN SEQUENCE OF 23-37, CIRCULAR DICHROISM ANALYSIS, AND PARTIAL
RP CHARACTERIZATION.
RC STRAIN=ATCC 33171 / DSM 3754 / JCM 8978 / NCIMB 764 / NRC 34002;
RX PubMed=12147354; DOI=10.1016/s0167-4838(02)00361-8;
RA Reindel S., Anemueller S., Sawaryn A., Matzanke B.F.;
RT "The DpsA-homologue of the archaeon Halobacterium salinarum is a
RT ferritin.";
RL Biochim. Biophys. Acta 1598:140-146(2002).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN
RP COMPLEX WITH IRON, AND SUBUNIT.
RX PubMed=15365182; DOI=10.1073/pnas.0401821101;
RA Zeth K., Offermann S., Essen L.-O., Oesterhelt D.;
RT "Iron-oxo clusters biomineralizing on protein surfaces: structural analysis
RT of Halobacterium salinarum DpsA in its low- and high-iron states.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13780-13785(2004).
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). {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: Homododecamer. The 12 subunits form a hollow sphere into which
CC the mineral iron core of up to 110 Fe(3+) can be deposited.
CC {ECO:0000269|PubMed:15365182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: The dps dodecamer comprises iron-binding sites for iron
CC translocation, oxidation and nucleation. Fe(2+) atoms are initially
CC bound to the outer surface in proximity to the iron entry pore from
CC which they are translocated toward the inter-subunit ferroxidase
CC centers via two discrete steps. Iron oxidation proceeds by transient
CC formation of tri-iron ferroxidase centers and Fe(3+) atoms move to two
CC distinct iron nucleation centers where iron mineralization occurs.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AE004437; AAG20524.1; -; Genomic_DNA.
DR PIR; H84394; H84394.
DR RefSeq; WP_010903826.1; NC_002607.1.
DR PDB; 1MOJ; X-ray; 1.90 A; A/B/C/D=1-182.
DR PDB; 1TJO; X-ray; 1.60 A; A/B/C/D=1-182.
DR PDB; 1TK6; X-ray; 2.20 A; A/B/C/D=1-182.
DR PDB; 1TKO; X-ray; 2.90 A; A/B/C/D=1-182.
DR PDB; 1TKP; X-ray; 2.20 A; A/B/C/D=1-182.
DR PDBsum; 1MOJ; -.
DR PDBsum; 1TJO; -.
DR PDBsum; 1TK6; -.
DR PDBsum; 1TKO; -.
DR PDBsum; 1TKP; -.
DR AlphaFoldDB; Q9HMP7; -.
DR SMR; Q9HMP7; -.
DR STRING; 64091.VNG_2443G; -.
DR PaxDb; Q9HMP7; -.
DR EnsemblBacteria; AAG20524; AAG20524; VNG_2443G.
DR GeneID; 5953388; -.
DR GeneID; 62887690; -.
DR KEGG; hal:VNG_2443G; -.
DR PATRIC; fig|64091.14.peg.1892; -.
DR HOGENOM; CLU_098183_0_1_2; -.
DR InParanoid; Q9HMP7; -.
DR OMA; KKYHWDV; -.
DR OrthoDB; 102179at2157; -.
DR PhylomeDB; Q9HMP7; -.
DR BRENDA; 1.16.3.2; 2552.
DR EvolutionaryTrace; Q9HMP7; -.
DR Proteomes; UP000000554; 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 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..182
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000201656"
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 /evidence="ECO:0000269|PubMed:15365182"
FT BINDING 79
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:15365182"
FT BINDING 83
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:15365182"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT SITE 53
FT /note="Involved in iron translocation"
FT SITE 56
FT /note="Involved in iron translocation"
FT SITE 75
FT /note="Involved in iron nucleation"
FT SITE 85
FT /note="Involved in iron translocation"
FT SITE 86
FT /note="Involved in iron translocation"
FT SITE 154
FT /note="Involved in iron nucleation"
FT SITE 164
FT /note="Involved in iron translocation"
FT SITE 168
FT /note="Involved in iron translocation"
FT SITE 171
FT /note="Involved in iron translocation"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:1TJO"
FT HELIX 24..54
FT /evidence="ECO:0007829|PDB:1TJO"
FT HELIX 60..87
FT /evidence="ECO:0007829|PDB:1TJO"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:1TJO"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1TJO"
FT HELIX 115..142
FT /evidence="ECO:0007829|PDB:1TJO"
FT HELIX 146..169
FT /evidence="ECO:0007829|PDB:1TJO"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1TJO"
SQ SEQUENCE 182 AA; 20100 MW; BC1EA5E7C5F61636 CRC64;
MSTQKNARAT AGEVEGSDAL RMDADRAEQC VDALNADLAN VYVLYHQLKK HHWNVEGAEF
RDLHLFLGEA AETAEEVADE LAERVQALGG VPHASPETLQ AEASVDVEDE DVYDIRTSLA
NDMAIYGDII EATREHTELA ENLGDHATAH MLREGLIELE DDAHHIEHYL EDDTLVTQGA
LE
