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Conserved domains on  [gi|1281363630|gb|ATY45211|]
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Bacterioferritin [Acinetobacter baumannii AB307-0294]

Protein Classification

bacterioferritin( domain architecture ID 10097036)

bacterioferritin regulates iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 3-154 1.04e-69

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.


:

Pssm-ID: 153099  Cd Length: 153  Bit Score: 207.01  E-value: 1.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   3 GNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHRED-INVGTD 81
Cdd:cd00907     2 GDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGkLRIGED 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLsDTEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:cd00907    82 VPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEIL-EDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 3-154 1.04e-69

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.


Pssm-ID: 153099  Cd Length: 153  Bit Score: 207.01  E-value: 1.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   3 GNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHRED-INVGTD 81
Cdd:cd00907     2 GDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGkLRIGED 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLsDTEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:cd00907    82 VPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEIL-EDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 1.71e-67

Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];


Pssm-ID: 441796  Cd Length: 152  Bit Score: 201.58  E-value: 1.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   3 GNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNM-HREDINVGTD 81
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLqDLGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLSDtEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED-EEEHIDWLETQLELIEKIGLQNYLQSQM 152
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-154 4.80e-43

bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 162022  Cd Length: 157  Bit Score: 139.56  E-value: 4.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   1 MRGNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHR-EDINVG 79
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDlGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281363630  80 TDVVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLSDTEEdHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEE-HIDWLETQLELIDKLGLENYLQAQV 154
PRK10635 PRK10635
bacterioferritin; Provisional
 1-154 2.68e-38

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 127.64  E-value: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   1 MRGNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHR-EDINVG 79
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDlGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281363630  80 TDVVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLSDtEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILAD-EEGHIDWLETELDLIGKLGLQNYLQSQI 154
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 1.15e-31

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


Pssm-ID: 459712  Cd Length: 141  Bit Score: 110.07  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   8 IDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHREDI------NVGTD 81
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELlaieapPSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLsDTEEDHTYWLEKQLRLIEL 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFL-DEQEEHEWFLEALLEKLER 141
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
47-129 1.00e-04

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 40.32  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630  47 EMQEEAS-HADAIIRRVLFLGAKP-----NMHR------EDINVgTDVVSCLKADLALEYHVREKLATGIKLCEEKGDYI 114
Cdd:NF041388   63 EAAEDAEeAADELAERAQALGGVPvsgpaALEEhapvepEGEDV-YDIRTSLENDLEMYGDIIESVRDHIELAENLGDHA 141

                          90
                  ....*....|....*
gi 1281363630 115 SRDMLRQQLSDTEED 129
Cdd:NF041388  142 TAELLREQLVELEED 156
 
Name Accession Description Interval E-value
Bacterioferritin cd00907
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ...
 3-154 1.04e-69

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.


Pssm-ID: 153099  Cd Length: 153  Bit Score: 207.01  E-value: 1.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   3 GNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHRED-INVGTD 81
Cdd:cd00907     2 GDPKVIEALNKALTGELTAINQYFLHARMLEDWGLEKLAERFRKESIEEMKHADKLIERILFLEGLPNLQRLGkLRIGED 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLsDTEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:cd00907    82 VPEMLENDLALEYEAIAALNEAIALCEEVGDYVSRDLLEEIL-EDEEEHIDWLETQLDLIDKMGLQNYLQSQM 153
Bfr COG2193
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];
3-154 1.71e-67

Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism];


Pssm-ID: 441796  Cd Length: 152  Bit Score: 201.58  E-value: 1.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   3 GNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNM-HREDINVGTD 81
Cdd:COG2193     1 GDPKVIELLNKALANELTAINQYFLHARMLKNWGLEKLAEKFYEESIEEMKHADKLIERILFLGGLPNLqDLGKLRIGED 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLSDtEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:COG2193    81 VEEMLECDLALELEAIALYREAIALCEEVGDYVSRDLLEEILED-EEEHIDWLETQLELIEKIGLQNYLQSQM 152
bfr TIGR00754
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ...
 1-154 4.80e-43

bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 162022  Cd Length: 157  Bit Score: 139.56  E-value: 4.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   1 MRGNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHR-EDINVG 79
Cdd:TIGR00754   1 MKGDPDVIQHLNKQLTNELTAINQYFLHARMQKNWGLKELADHEYHESIDEMKHADEIIERILFLEGLPNLQDlGKLRIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281363630  80 TDVVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLSDTEEdHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:TIGR00754  81 ETVREMLEADLALELDVLNRLKEAIAYAEEVRDYVSRDLLEEILEDEEE-HIDWLETQLELIDKLGLENYLQAQV 154
PRK10635 PRK10635
bacterioferritin; Provisional
 1-154 2.68e-38

bacterioferritin; Provisional


Pssm-ID: 182604  Cd Length: 158  Bit Score: 127.64  E-value: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   1 MRGNPEVIDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHR-EDINVG 79
Cdd:PRK10635    1 MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLMRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDlGKLNIG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281363630  80 TDVVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLSDtEEDHTYWLEKQLRLIELIGLQNYIQSQI 154
Cdd:PRK10635   81 EDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILAD-EEGHIDWLETELDLIGKLGLQNYLQSQI 154
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 8-143 1.15e-31

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


Pssm-ID: 459712  Cd Length: 141  Bit Score: 110.07  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   8 IDYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIDHEMQEEASHADAIIRRVLFLGAKPNMHREDI------NVGTD 81
Cdd:pfam00210   1 IAALNEQLADELTASYQYLQMHWYVKGPGFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNGTRVELlaieapPSFGS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEEKGDYISRDMLRQQLsDTEEDHTYWLEKQLRLIEL 143
Cdd:pfam00210  81 VLEVLEAALEHEKKVTKSLRELIELAEEEGDYATADFLQWFL-DEQEEHEWFLEALLEKLER 141
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 9-138 3.37e-11

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 57.12  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630   9 DYLNMLIGGELAARDQYLIHSRMYEDWGLNKIYERIdheMQEEASHADAIIRRVLFLGAKPNMHR-------EDINVGTD 81
Cdd:cd00657     1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEI---ADEERRHADALAERLRELGGTPPLPPahllaayALPKTSDD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1281363630  82 VVSCLKADLALEYHVREKLATGIKLCEekgDYISRDMLRQQLSDtEEDHTYWLEKQL 138
Cdd:cd00657    78 PAEALRAALEVEARAIAAYRELIEQAD---DPELRRLLERILAD-EQRHAAWFRKLL 130
DNAstvprot_Halo NF041388
DNA starvation/stationary phase protection protein DpsA;
47-129 1.00e-04

DNA starvation/stationary phase protection protein DpsA;


Pssm-ID: 469279 [Multi-domain]  Cd Length: 171  Bit Score: 40.32  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281363630  47 EMQEEAS-HADAIIRRVLFLGAKP-----NMHR------EDINVgTDVVSCLKADLALEYHVREKLATGIKLCEEKGDYI 114
Cdd:NF041388   63 EAAEDAEeAADELAERAQALGGVPvsgpaALEEhapvepEGEDV-YDIRTSLENDLEMYGDIIESVRDHIELAENLGDHA 141

                          90
                  ....*....|....*
gi 1281363630 115 SRDMLRQQLSDTEED 129
Cdd:NF041388  142 TAELLREQLVELEED 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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