DPS_LISMO
ID DPS_LISMO Reviewed; 156 AA.
AC Q8Y8G1; Q9F425;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
DE AltName: Full=Ferritin-like protein;
DE AltName: Full=Non-heme iron-containing ferritin;
GN Name=dps; Synonyms=flp, fri; OrderedLocusNames=lmo0943;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-147, AND PROTEIN SEQUENCE OF 1-22.
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=10981685; DOI=10.1111/j.1574-6968.2000.tb09257.x;
RA Hebraud M., Guzzo J.;
RT "The main cold shock protein of Listeria monocytogenes belongs to the
RT family of ferritin-like proteins.";
RL FEMS Microbiol. Lett. 190:29-34(2000).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=LM1;
RX PubMed=12383509; DOI=10.1016/s0378-1119(02)00839-9;
RA Polidoro M., De Biase D., Montagnini B., Guarrera L., Cavallo S.,
RA Valenti P., Stefanini S., Chiancone E.;
RT "The expression of the dodecameric ferritin in Listeria spp. is induced by
RT iron limitation and stationary growth phase.";
RL Gene 296:121-128(2002).
RN [4]
RP FUNCTION IN PROTECTION AGAINST MULTIPLE STRESSES, AND REQUIREMENT FOR
RP VIRULENCE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=16098690; DOI=10.1016/j.femsle.2005.07.015;
RA Dussurget O., Dumas E., Archambaud C., Chafsey I., Chambon C., Hebraud M.,
RA Cossart P.;
RT "Listeria monocytogenes ferritin protects against multiple stresses and is
RT required for virulence.";
RL FEMS Microbiol. Lett. 250:253-261(2005).
RN [5]
RP FUNCTION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=15758237; DOI=10.1099/mic.0.27552-0;
RA Olsen K.N., Larsen M.H., Gahan C.G., Kallipolitis B., Wolf X.A., Rea R.,
RA Hill C., Ingmer H.;
RT "The Dps-like protein Fri of Listeria monocytogenes promotes stress
RT tolerance and intracellular multiplication in macrophage-like cells.";
RL Microbiology 151:925-933(2005).
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. Does
CC not bind to DNA (By similarity). Dps is important for full resistance
CC to heat and cold shocks and is essential for full virulence of this
CC bacterium. It seems to play a direct or indirect role on the production
CC and/or stability of listeriolysin O. {ECO:0000250,
CC ECO:0000269|PubMed:12383509, ECO:0000269|PubMed:15758237,
CC ECO:0000269|PubMed:16098690}.
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 500 Fe(3+) can be deposited (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By iron limitation and stationary growth phase.
CC {ECO:0000269|PubMed:12383509}.
CC -!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the interfaces
CC between subunits related by 2-fold symmetry axes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AL591977; CAC99021.1; -; Genomic_DNA.
DR EMBL; AJ401090; CAC08216.1; -; Genomic_DNA.
DR PIR; AG1192; AG1192.
DR RefSeq; NP_464468.1; NC_003210.1.
DR RefSeq; WP_003719147.1; NZ_CP023861.1.
DR PDB; 2IY4; X-ray; 2.31 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y=1-156.
DR PDBsum; 2IY4; -.
DR AlphaFoldDB; Q8Y8G1; -.
DR SMR; Q8Y8G1; -.
DR STRING; 169963.lmo0943; -.
DR PaxDb; Q8Y8G1; -.
DR EnsemblBacteria; CAC99021; CAC99021; CAC99021.
DR GeneID; 57075870; -.
DR GeneID; 986847; -.
DR KEGG; lmo:lmo0943; -.
DR PATRIC; fig|169963.11.peg.970; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_4_0_9; -.
DR OMA; LYLQTHN; -.
DR PhylomeDB; Q8Y8G1; -.
DR BioCyc; LMON169963:LMO0943-MON; -.
DR EvolutionaryTrace; Q8Y8G1; -.
DR Proteomes; UP000000817; 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 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.
DR PROSITE; PS00819; DPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Iron; Iron storage;
KW Metal-binding; Oxidoreductase; Reference proteome; Virulence.
FT CHAIN 1..156
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000201658"
FT BINDING 31
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 58
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 62
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 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="V -> I (in Ref. 2; CAC08216)"
FT /evidence="ECO:0000305"
FT HELIX 7..33
FT /evidence="ECO:0007829|PDB:2IY4"
FT HELIX 39..66
FT /evidence="ECO:0007829|PDB:2IY4"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:2IY4"
FT HELIX 95..123
FT /evidence="ECO:0007829|PDB:2IY4"
FT HELIX 126..149
FT /evidence="ECO:0007829|PDB:2IY4"
SQ SEQUENCE 156 AA; 18048 MW; BF29E2C91DADBC58 CRC64;
MKTINSVDTK EFLNHQVANL NVFTVKIHQI HWYMRGHNFF TLHEKMDDLY SEFGEQMDEV
AERLLAIGGS PFSTLKEFLE NASVEEAPYT KPKTMDQLME DLVGTLELLR DEYQQGIELT
DKEGDNVTND MLIAFKASID KHIWMFKAFL GKAPLE
