DPS_MYCS2
ID DPS_MYCS2 Reviewed; 183 AA.
AC A0R692; I7GFT5; Q8VP75;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; OrderedLocusNames=MSMEG_6467, MSMEI_6295;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP INDUCTION, AND INTERACTION WITH DNA.
RX PubMed=12082169; DOI=10.1093/protein/15.6.503;
RA Gupta S., Pandit S.B., Srinivasan N., Chatterji D.;
RT "Proteomics analysis of carbon-starved Mycobacterium smegmatis: induction
RT of Dps-like protein.";
RL Protein Eng. 15:503-512(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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 protects DNA from hydroxyl radical-mediated cleavage.
CC Binds DNA with no apparent sequence specificity without self-
CC aggregation nor promotion of DNA condensation. Is unable to protect DNA
CC from DNase-mediated cleavage (By 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 identical subunits form a hollow sphere into which the
CC mineral iron core of up to 500 Fe(3+) can be deposited. Homododecamer.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}.
CC -!- INDUCTION: Expressed preferentially under carbon starvation.
CC {ECO:0000269|PubMed:12082169}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY065628; AAL40885.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK75435.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42721.1; -; Genomic_DNA.
DR RefSeq; WP_003897878.1; NZ_SIJM01000033.1.
DR RefSeq; YP_890680.1; NC_008596.1.
DR PDB; 5H46; X-ray; 2.85 A; A=9-157.
DR PDBsum; 5H46; -.
DR AlphaFoldDB; A0R692; -.
DR SMR; A0R692; -.
DR STRING; 246196.MSMEI_6295; -.
DR PRIDE; A0R692; -.
DR EnsemblBacteria; ABK75435; ABK75435; MSMEG_6467.
DR EnsemblBacteria; AFP42721; AFP42721; MSMEI_6295.
DR GeneID; 66737739; -.
DR KEGG; msg:MSMEI_6295; -.
DR KEGG; msm:MSMEG_6467; -.
DR PATRIC; fig|246196.19.peg.6290; -.
DR eggNOG; COG0783; Bacteria.
DR OMA; DDYSIGR; -.
DR OrthoDB; 1742631at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..183
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000293598"
FT REGION 162..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
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 66
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 70
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 70
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 13..41
FT /evidence="ECO:0007829|PDB:5H46"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5H46"
FT HELIX 48..75
FT /evidence="ECO:0007829|PDB:5H46"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:5H46"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5H46"
FT HELIX 102..127
FT /evidence="ECO:0007829|PDB:5H46"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5H46"
FT HELIX 132..156
FT /evidence="ECO:0007829|PDB:5H46"
SQ SEQUENCE 183 AA; 20270 MW; 3ACB34B43B23F877 CRC64;
MTSFTIPGLS DKKASDVADL LQKQLSTYND LHLTLKHVHW NVVGPNFIGV HEMIDPQVEL
VRGYADEVAE RIATLGKSPK GTPGAIIKDR TWDDYSVERD TVQAHLAALD LVYNGVIEDT
RKSIEKLEDL DLVSQDLLIA HAGELEKFQW FVRAHLESAG GQLTHEGQST EKGAADKARR
KSA
