DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   9 KELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEA-GK 87
Cdd:cd01043     1 EALNQLLADLYVLYLKLKNYHWNVKGPNFFALHELFEELYDELREAIDEIAERIRALGGKPLGTLKEYAELSTIKEEpAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631507760  88 NYSAEQMVEAFSNDLTHISEQLVKSIEVAGEAGDDVSEDMFIGMKNSVDKHNWMFKSYL 146
Cdd:cd01043    81 VLSAKEMVAELLEDYETLIEELREAIELADEAGDPATADLLTEIIRELEKQAWMLRAHL 139

DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   9 KELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEA-GK 87
Cdd:cd01043     1 EALNQLLADLYVLYLKLKNYHWNVKGPNFFALHELFEELYDELREAIDEIAERIRALGGKPLGTLKEYAELSTIKEEpAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631507760  88 NYSAEQMVEAFSNDLTHISEQLVKSIEVAGEAGDDVSEDMFIGMKNSVDKHNWMFKSYL 146
Cdd:cd01043    81 VLSAKEMVAELLEDYETLIEELREAIELADEAGDPATADLLTEIIRELEKQAWMLRAHL 139

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   8 VKELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEAGk 87
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAPPSFG- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631507760  88 nySAEQMVEAFSNDLTHISEQLVKSIEVAGEAGDDVSEDMFIGMKNSVDKHNWMFKSYL 146
Cdd:pfam00210  80 --SVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALL 136

DNA starvation/stationary phase protection protein DpsA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   7 VVKELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEAG 86
Cdd:NF041388   24 IVDALNTDLAATYVLYHQLKKHHWNVEGAEFRDLHLFLGEAAEDAEEAADELAERAQALGGVPVSGPAALEEHAPVEPEG 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1631507760  87 KN-YSAEQMVEafsNDLT---HISEQLVKSIEVAGEAGDDVSEDM 127
Cdd:NF041388  104 EDvYDIRTSLE---NDLEmygDIIESVRDHIELAENLGDHATAEL 145

DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   9 KELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEA-GK 87
Cdd:cd01043     1 EALNQLLADLYVLYLKLKNYHWNVKGPNFFALHELFEELYDELREAIDEIAERIRALGGKPLGTLKEYAELSTIKEEpAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631507760  88 NYSAEQMVEAFSNDLTHISEQLVKSIEVAGEAGDDVSEDMFIGMKNSVDKHNWMFKSYL 146
Cdd:cd01043    81 VLSAKEMVAELLEDYETLIEELREAIELADEAGDPATADLLTEIIRELEKQAWMLRAHL 139

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   8 VKELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEAGk 87
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELLAIEAPPSFG- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631507760  88 nySAEQMVEAFSNDLTHISEQLVKSIEVAGEAGDDVSEDMFIGMKNSVDKHNWMFKSYL 146
Cdd:pfam00210  80 --SVLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFLDEQEEHEWFLEALL 136

DNA starvation/stationary phase protection protein DpsA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760   7 VVKELNQQVANWTVAYTKLHNFHWYVKGPNFFSLHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEISIVDEAG 86
Cdd:NF041388   24 IVDALNTDLAATYVLYHQLKKHHWNVEGAEFRDLHLFLGEAAEDAEEAADELAERAQALGGVPVSGPAALEEHAPVEPEG 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1631507760  87 KN-YSAEQMVEafsNDLT---HISEQLVKSIEVAGEAGDDVSEDM 127
Cdd:NF041388  104 EDvYDIRTSLE---NDLEmygDIIESVRDHIELAENLGDHATAEL 145

Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631507760  40 LHEKFEELYNEASQYVDDLAERILAIGGNPVGTLKESLEIsivdeagknysAEQMVEAFSNDLT---HISEQLVKSIEVA 116
Cdd:cd00907    39 LAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGKLRI-----------GEDVPEMLENDLAleyEAIAALNEAIALC 107

                          90       100
                  ....*....|....*....|..
gi 1631507760 117 GEAGDDVSEDMFIGMKNSVDKH 138
Cdd:cd00907   108 EEVGDYVSRDLLEEILEDEEEH 129