DPS_PORGI
ID DPS_PORGI Reviewed; 159 AA.
AC P0C935; Q7MXS1; Q9WXJ3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; OrderedLocusNames=PG_0090;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: Responsible for protection of cells against peroxide,
CC especially against hydrogen peroxide. Required for survival in host
CC cells. Although it binds iron, it may not contribute to iron storage.
CC The iron-loaded dps has DNA-binding activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Constitutively expressed but is up-regulated by exposure to
CC atomospheric oxygen in an OxyR-dependent manner.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AE015924; AAQ65337.1; -; Genomic_DNA.
DR RefSeq; WP_005873985.1; NC_002950.2.
DR AlphaFoldDB; P0C935; -.
DR SMR; P0C935; -.
DR STRING; 242619.PG_0090; -.
DR EnsemblBacteria; AAQ65337; AAQ65337; PG_0090.
DR KEGG; pgi:PG_0090; -.
DR PATRIC; fig|242619.8.peg.81; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_2_2_10; -.
DR OMA; LYLQTHN; -.
DR OrthoDB; 1742631at2; -.
DR BioCyc; PGIN242619:G1G02-82-MON; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..159
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253334"
FT BINDING 40
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 67
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 71
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 71
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 159 AA; 17865 MW; 60889B904D331AC6 CRC64;
MKKILEVTGL KEQQVAPVVK GLSGLLADLQ VYYSNLRGFH WNIRGAEFFV LHEQYEKMYD
DLAGKIDEVA ERILQLGGKP ENRFSEYLKV AEVKEEHELV CAASTLKNVT DTLQIIMAKE
RAIAEVAGEA GDEVTVDLMI GFLSEQEKLV WMLSAYAAK