DPS_HELPY
ID DPS_HELPY Reviewed; 144 AA.
AC P43313; Q64EY0; Q932V4; Q9F7B4; Q9F7B5; Q9F7B6; Q9F7B7; Q9F7B8; Q9F7B9;
AC Q9K2M7; Q9K2U7; Q9KW50; Q9L762; Q9L763; Q9L764; Q9L765; Q9L766;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
DE AltName: Full=Bacterioferritin;
DE AltName: Full=HP-NAP;
DE AltName: Full=Neutrophil-activating protein A;
DE Short=NAP A;
GN Name=dps; Synonyms=napA; OrderedLocusNames=HP_0243;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-66.
RC STRAIN=8826;
RX PubMed=7883175; DOI=10.1016/0378-1119(94)00774-m;
RA Evans D.J. Jr., Evans D.G., Lampert H.C., Nakano H.;
RT "Identification of four new prokaryotic bacterioferritins, from
RT Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema
RT pallidum, by analysis of gene sequences.";
RL Gene 153:123-127(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN NEUTROPHIL ACTIVATION.
RC STRAIN=Isolate 96T/FRE, Isolate 96T/HAR, Isolate 96T/KAD, Isolate 96T/NEW,
RC Isolate 96T/ROS, and Isolate 96T/THO;
RX PubMed=11069248; DOI=10.1086/317611;
RA Leakey A., La Brooy J., Hirst R.;
RT "The ability of Helicobacter pylori to activate neutrophils is determined
RT by factors other than H. pylori neutrophil-activating protein.";
RL J. Infect. Dis. 182:1749-1755(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1811a, 2A, 2B, 5060d, 5A, 5D, DB2, G21, RHP901a, and SS1;
RA Dundon W.G., Guidotti S., Covacci A., Rappuoli R., Montecucco C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YS2, and YS8;
RA Nozawa R.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MI 355, and MI 356;
RA Dundon W.G., Carroll I., Marshall D.G., O'Morain C.A., Smyth C.J.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MEL-HP27;
RA Duan G., Kang Q.;
RT "The napA gene sequence of Helicobacter pylori MEL-HP27 strain isolated
RT from central China.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Y06;
RA Yuan W., Yan J., Mao Y.F.;
RT "Construction of prokaryotic expression system of Helicobacter pylori napA
RT gene and immunity and inflammation-induced effect of the expressed
RT product.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RA Jun L., Min L., Guo L.-B., Yan L.;
RT "Construction of prokaryotic expression system of Helicobacter pylori napA
RT gene and immunity- and inflammation-induced effect of the expressed
RT product.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [10]
RP PROTEIN SEQUENCE OF 1-17, AND BINDING TO SULFATED CARBOHYDRATES IN MUCIN.
RC STRAIN=3B3, and ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=9453593; DOI=10.1128/iai.66.2.444-447.1998;
RA Namavar F., Sparrius M., Veerman E.C., Appelmelk B.J.,
RA Vandenbroucke-Grauls C.M.;
RT "Neutrophil-activating protein mediates adhesion of Helicobacter pylori to
RT sulfated carbohydrates on high-molecular-weight salivary mucin.";
RL Infect. Immun. 66:444-447(1998).
RN [11]
RP FUNCTION IN NEUTROPHIL ACTIVATION.
RX PubMed=7768601; DOI=10.1128/iai.63.6.2213-2220.1995;
RA Evans D.J. Jr., Evans D.G., Takemura T., Nakano H., Lampert H.C.,
RA Graham D.Y., Granger D.N., Kvietys P.R.;
RT "Characterization of a Helicobacter pylori neutrophil-activating protein.";
RL Infect. Immun. 63:2213-2220(1995).
RN [12]
RP BINDING TO NEUTROPHIL GLYCOSPHINGOLIPIDS.
RX PubMed=9228091; DOI=10.1074/jbc.272.30.19067;
RA Teneberg S., Miller-Podraza H., Lampert H.C., Evans D.J. Jr., Evans D.G.,
RA Danielsson D., Karlsson K.A.;
RT "Carbohydrate binding specificity of the neutrophil-activating protein of
RT Helicobacter pylori.";
RL J. Biol. Chem. 272:19067-19071(1997).
RN [13]
RP BINDING TO IRON, AND SUBUNIT.
RX PubMed=10564468; DOI=10.1046/j.1365-2958.1999.01584.x;
RA Tonello F., Dundon W.G., Satin B., Molinari M., Tognon G., Grandi G.,
RA Del Giudice G., Rappuoli R., Montecucco C.;
RT "The Helicobacter pylori neutrophil-activating protein is an iron-binding
RT protein with dodecameric structure.";
RL Mol. Microbiol. 34:238-246(1999).
RN [14]
RP FUNCTION IN ACTIVATION OF NEUTROPHILS AND MONOCYTES.
RX PubMed=10790422; DOI=10.1084/jem.191.9.1467;
RA Satin B., Del Giudice G., Della Bianca V., Dusi S., Laudanna C.,
RA Tonello F., Kelleher D., Rappuoli R., Montecucco C., Rossi F.;
RT "The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a
RT protective antigen and a major virulence factor.";
RL J. Exp. Med. 191:1467-1476(2000).
RN [15]
RP FUNCTION IN ACTIVATION OF MAST CELLS.
RX PubMed=11857341;
RX DOI=10.1002/1521-4141(200203)32:3<671::aid-immu671>3.3.co;2-x;
RA Montemurro P., Nishioka H., Dundon W.G., de Bernard M., Del Giudice G.,
RA Rappuoli R., Montecucco C.;
RT "The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a
RT potent stimulant of mast cells.";
RL Eur. J. Immunol. 32:671-676(2002).
RN [16]
RP FUNCTION IN ACTIVATION OF THE MAPK PATHWAY IN HUMAN NEUTROPHILS.
RX PubMed=12672049; DOI=10.1002/eji.200323726;
RA Nishioka H., Baesso I., Semenzato G., Trentin L., Rappuoli R.,
RA Del Giudice G., Montecucco C.;
RT "The neutrophil-activating protein of Helicobacter pylori (HP-NAP)
RT activates the MAPK pathway in human neutrophils.";
RL Eur. J. Immunol. 33:840-849(2003).
RN [17]
RP INTERACTION WITH DNA, FUNCTION IN PROTECTION FROM OXIDATIVE STRESS, AND
RP REGULATION.
RX PubMed=12748264; DOI=10.1099/jmm.0.05070-0;
RA Cooksley C., Jenks P.J., Green A., Cockayne A., Logan R.P.H., Hardie K.R.;
RT "NapA protects Helicobacter pylori from oxidative stress damage, and its
RT production is influenced by the ferric uptake regulator.";
RL J. Med. Microbiol. 52:461-469(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH IRON, AND SUBUNIT.
RX PubMed=12368104; DOI=10.1016/s0022-2836(02)00879-3;
RA Zanotti G., Papinutto E., Dundon W., Battistutta R., Seveso M.,
RA Del Giudice G., Rappuoli R., Montecucco C.;
RT "Structure of the neutrophil-activating protein from Helicobacter pylori.";
RL J. Mol. Biol. 323:125-130(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). Required for the survival in the presence of oxidative
CC stress. Dps is also a virulence factor that activates neutrophils, mast
CC cells and monocytes. It binds to neutrophil-glycosphingolipids and to
CC sulfated carbohydrates on mucin. It might have a role in the
CC accumulation of neutrophils and monocytes at the site of infection.
CC Induces superoxide anion generation, adhesion and chemotaxis of
CC neutrophils, through a pertussis toxin-sensitive pathway involving MAP
CC kinases. {ECO:0000250, ECO:0000269|PubMed:10790422,
CC ECO:0000269|PubMed:11069248, ECO:0000269|PubMed:11857341,
CC ECO:0000269|PubMed:12672049, ECO:0000269|PubMed:12748264,
CC ECO:0000269|PubMed:7768601}.
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.
CC {ECO:0000269|PubMed:10564468, ECO:0000269|PubMed:12368104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the interfaces
CC between subunits related by 2-fold symmetry axes. {ECO:0000250}.
CC -!- MISCELLANEOUS: According to PubMed:12672049, colocalizes with DNA but
CC according to PubMed:9228091 it does not interact with DNA.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; U16121; AAA67928.1; -; Genomic_DNA.
DR EMBL; AF284116; AAG28154.1; -; Genomic_DNA.
DR EMBL; AF284117; AAG28155.1; -; Genomic_DNA.
DR EMBL; AF284118; AAG28156.1; -; Genomic_DNA.
DR EMBL; AF284119; AAG28157.1; -; Genomic_DNA.
DR EMBL; AF284120; AAG28158.1; -; Genomic_DNA.
DR EMBL; AF284121; AAG28159.1; -; Genomic_DNA.
DR EMBL; AF227072; AAF37840.1; -; Genomic_DNA.
DR EMBL; AF227073; AAF37841.1; -; Genomic_DNA.
DR EMBL; AF227074; AAF37842.1; -; Genomic_DNA.
DR EMBL; AF227075; AAF37843.1; -; Genomic_DNA.
DR EMBL; AF227076; AAF37844.1; -; Genomic_DNA.
DR EMBL; AF227077; AAF37845.1; -; Genomic_DNA.
DR EMBL; AF227078; AAF37846.1; -; Genomic_DNA.
DR EMBL; AF227079; AAF37847.1; -; Genomic_DNA.
DR EMBL; AF227080; AAF37848.1; -; Genomic_DNA.
DR EMBL; AF227081; AAF37849.1; -; Genomic_DNA.
DR EMBL; AB045142; BAA96879.1; -; Genomic_DNA.
DR EMBL; AB045143; BAA96880.1; -; Genomic_DNA.
DR EMBL; AF432415; AAL27478.1; -; Genomic_DNA.
DR EMBL; AF432416; AAL27479.1; -; Genomic_DNA.
DR EMBL; AY366361; AAQ72432.1; -; Genomic_DNA.
DR EMBL; AY714227; AAU21203.1; -; Genomic_DNA.
DR EMBL; DQ341279; ABC68518.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07308.1; -; Genomic_DNA.
DR PIR; C64550; C64550.
DR RefSeq; NP_207041.1; NC_000915.1.
DR RefSeq; WP_000846461.1; NC_018939.1.
DR PDB; 1JI4; X-ray; 2.52 A; A/B/C/D/E/F/G/H/I/J/K/L=1-144.
DR PDBsum; 1JI4; -.
DR AlphaFoldDB; P43313; -.
DR SMR; P43313; -.
DR DIP; DIP-3296N; -.
DR IntAct; P43313; 5.
DR MINT; P43313; -.
DR STRING; 85962.C694_01230; -.
DR PaxDb; P43313; -.
DR PRIDE; P43313; -.
DR EnsemblBacteria; AAD07308; AAD07308; HP_0243.
DR KEGG; hpy:HP_0243; -.
DR PATRIC; fig|85962.47.peg.263; -.
DR eggNOG; COG0783; Bacteria.
DR OMA; LYLQTHN; -.
DR PhylomeDB; P43313; -.
DR EvolutionaryTrace; P43313; -.
DR Proteomes; UP000000429; 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..144
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000201662"
FT BINDING 25
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:0000269|PubMed:12368104"
FT BINDING 52
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:0000269|PubMed:12368104"
FT BINDING 56
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:0000269|PubMed:12368104"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT VARIANT 9
FT /note="H -> V (in strain: Isolate 96T/FRE)"
FT VARIANT 35
FT /note="N -> H (in strain: Y06)"
FT VARIANT 46
FT /note="E -> G (in strain: 5060d, YS8 and Isolate 96T/KAD)"
FT VARIANT 50
FT /note="M -> L (in strain: G21)"
FT VARIANT 55..56
FT /note="AE -> EK (in strain: Isolate 96T/ROS)"
FT VARIANT 58
FT /note="I -> L (in strain: 8826)"
FT VARIANT 59
FT /note="V -> A (in strain: SS1, G21, YS8, Isolate 96T/THO,
FT Isolate 96T/ROS and Isolate 96T/HAR)"
FT VARIANT 70
FT /note="S -> T (in strain: 1811a and YS2)"
FT VARIANT 73
FT /note="I -> L (in strain: 8826, SS1, RHO901a, G21, 1811a,
FT 5060d, YS2, YS8, Y06, Isolate 96T/THO, Isolate 96T/ROS,
FT Isolate 96T/KAD, Isolate 96T/FRE and Isolate 96T/HAR)"
FT VARIANT 80
FT /note="E -> D (in strain: 8826)"
FT VARIANT 95..97
FT /note="ILE -> FLG (in strain: G21)"
FT VARIANT 97
FT /note="E -> D (in strain: Isolate 96T/ROS)"
FT VARIANT 97
FT /note="E -> G (in strain: 8826, RHP901a, SS1, DB2, Y06,
FT Isolate 96T/THO and Isolate 96T/FRE)"
FT VARIANT 101
FT /note="Y -> H (in strain: 8826, SS1, DB2, RHP901a, G21, 2A,
FT 2B, 5A, 5D, 1811a, 5060d, YS2, YS8, MI 355, MI 356, MEL-
FT HP27, Y06, Isolate 96T/THO, Isolate 96T/ROS, Isolate 96T/
FT KAD, Isolate 96T/FRE, Isolate 96T/NEW, Isolate 96T/HAR and
FT ATCC 43629)"
FT VARIANT 107
FT /note="K -> E (in strain: Isolate 96T/KAD)"
FT VARIANT 140
FT /note="Q -> E (in strain: 8826, SS1, DB2, G21, MI 355, MI
FT 356 and Y06)"
FT CONFLICT 11
FT /note="Q -> G (in Ref. 9)"
FT /evidence="ECO:0000305"
FT HELIX 3..27
FT /evidence="ECO:0007829|PDB:1JI4"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1JI4"
FT HELIX 33..60
FT /evidence="ECO:0007829|PDB:1JI4"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1JI4"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:1JI4"
FT HELIX 119..142
FT /evidence="ECO:0007829|PDB:1JI4"
SQ SEQUENCE 144 AA; 16933 MW; D2EEBD4929A5096D CRC64;
MKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ
LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV
TVTYADDQLA KLQKSIWMLQ AHLA
