ID   DPS_PORG3               Reviewed;         159 AA.
AC   B2RMG0; Q7MXS1; Q9WXJ3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DNA protection during starvation protein;
DE            EC=1.16.-.-;
GN   Name=dps; OrderedLocusNames=PGN_2037;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, EXPRESSION,
RP   AND FUNCTION IN PROTECTION AGAINST HYDROGEN PEROXIDE.
RX   PubMed=12595429; DOI=10.1128/iai.71.3.1170-1178.2003;
RA   Ueshima J., Shoji M., Ratnayake D.B., Abe K., Yoshida S., Yamamoto K.,
RA   Nakayama K.;
RT   "Purification, gene cloning, gene expression, and mutants of Dps from the
RT   obligate anaerobe Porphyromonas gingivalis.";
RL   Infect. Immun. 71:1170-1178(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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.
CC       {ECO:0000269|PubMed:12595429}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000305}.
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; AB025779; BAA76886.1; -; Genomic_DNA.
DR   EMBL; AP009380; BAG34555.1; -; Genomic_DNA.
DR   RefSeq; WP_012458706.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RMG0; -.
DR   SMR; B2RMG0; -.
DR   STRING; 431947.PGN_2037; -.
DR   EnsemblBacteria; BAG34555; BAG34555; PGN_2037.
DR   GeneID; 29257172; -.
DR   KEGG; pgn:PGN_2037; -.
DR   eggNOG; COG0783; Bacteria.
DR   HOGENOM; CLU_098183_2_2_10; -.
DR   OMA; LYLQTHN; -.
DR   BioCyc; PGIN431947:G1G2V-2270-MON; -.
DR   Proteomes; UP000008842; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..159
FT                   /note="DNA protection during starvation protein"
FT                   /id="PRO_0000370693"
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"
FT   CONFLICT        158
FT                   /note="T -> A (in Ref. 1; BAA76886)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   159 AA;  17823 MW;  6094EB904D33184C CRC64;
     MKKILEVTGL KEQQVAPVVK GLSGLLADLQ VYYSNLRGFH WNIRGAEFFV LHEQYEKMYD
     DLAGKIDEVA ERILQLGGKP ENRFSEYLKV AEVKEEHELV CAASTLKNVT DTLQIIMAKE
     RAIAEVAGEA GDEVTVDLMI GFLSGQEKLV WMLSAYATK