DPS_SYNE7
ID DPS_SYNE7 Reviewed; 176 AA.
AC Q55024; Q31L68; Q7M1C4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
DE AltName: Full=Nutrient stress-induced DNA-binding protein;
GN Name=dps; Synonyms=dpsA; OrderedLocusNames=Synpcc7942_2171;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-61; 63-66; 68-69
RP AND 156-166, FUNCTION AS A CATALASE, AND HEME BINDING.
RX PubMed=7673237; DOI=10.1074/jbc.270.38.22478;
RA Pena M.M.O., Bullerjahn G.S.;
RT "The DpsA protein of Synechococcus sp. Strain PCC7942 is a DNA-binding
RT hemoprotein. Linkage of the Dps and bacterioferritin protein families.";
RL J. Biol. Chem. 270:22478-22482(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 3-71, DNA-BINDING, INDUCTION, AND SUBUNIT.
RX PubMed=7794101; DOI=10.1007/bf00404206;
RA Pena M.M.O., Burkhart W., Bullerjahn G.S.;
RT "Purification and characterization of a Synechococcus sp. strain PCC 7942
RT polypeptide structurally similar to the stress-induced Dps/PexB protein of
RT Escherichia coli.";
RL Arch. Microbiol. 163:337-344(1995).
RN [4]
RP SUBCELLULAR LOCATION, AND SUGGESTED FUNCTION.
RX PubMed=12442298;
RX DOI=10.1002/1521-4028(200212)42:6<367::aid-jobm367>3.0.co;2-t;
RA Durham K.A., Bullerjahn G.S.;
RT "Immunocytochemical localization of the stress-induced DpsA protein in the
RT cyanobacterium Synechococcus sp. strain PCC 7942.";
RL J. Basic Microbiol. 42:367-372(2002).
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). Dps binds the chromosome non-specifically, forming a
CC highly ordered and stable dps-DNA co-crystal within which chromosomal
CC DNA is condensed and protected from diverse damages. Soluble dps might
CC function in iron homeostasis under high iron concentration, while the
CC dps-DNA complex might associate with the protection of DNA from
CC oxidative stress at low iron concentration. Has a weak catalase
CC activity in vitro. {ECO:0000250, ECO:0000269|PubMed:7673237}.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme per molecule.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:7794101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12442298}. Note=The
CC dps-DNA complex is found in the cytoplasm whereas a soluble dps is
CC localized preferentially to the thylakoid membrane and is also found in
CC the cell envelope.
CC -!- INDUCTION: The dps-DNA complex accumulates during stationary phase and
CC under nitrogen, sulfur, and phosphate stress, but not under iron
CC limitation. {ECO:0000269|PubMed:7794101}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; U19762; AAA86318.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58201.1; -; Genomic_DNA.
DR PIR; A44631; A44631.
DR PIR; T48904; T48904.
DR RefSeq; WP_011244234.1; NC_007604.1.
DR AlphaFoldDB; Q55024; -.
DR SMR; Q55024; -.
DR STRING; 1140.Synpcc7942_2171; -.
DR PRIDE; Q55024; -.
DR EnsemblBacteria; ABB58201; ABB58201; Synpcc7942_2171.
DR KEGG; syf:Synpcc7942_2171; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_0_1_3; -.
DR OMA; AELCCFE; -.
DR OrthoDB; 1742631at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2171-MON; -.
DR GO; GO:0005737; C:cytoplasm; 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 SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00818; DPS_1; 1.
DR PROSITE; PS00819; DPS_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA condensation; DNA-binding; Heme;
KW Iron; Iron storage; Metal-binding; Oxidoreductase.
FT CHAIN 1..176
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000201655"
FT BINDING 50
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 78
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 81
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 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 71
FT /note="S -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="L -> F (in Ref. 1; AAA86318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 19659 MW; 06657E023372635D CRC64;
MTNTGLVQSF SQIEPNVLGL ETSVTSQICE GLNRALASFQ VLYLQYQKHH FTVQGAEFYS
LHEFFEDSYG SVKDHVHDLG ERLNGLGGVP VAHPLKLAEL TCFAIEEDGV FNCRTMLEHD
LAAEQAILSL LRRLTAQVES LGDRATRYLL EGILLKTEER AYHIAHFLAP DSLKLA
