hypothetical protein [uncultured marine bacterium MedDCM-OCT-S08-C1463]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
OM_channels super family | cl21487 | Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in ... |
194-310 | 1.75e-10 | |||
Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in strand and shear number. Classical (gram-negative ) porins are non-specific channels for small hydrophillic molecules and form 16 beta-stranded barrels (16,20), which associate as trimers. Maltoporin-like channels have specificities for various sugars and form 18 beta-stranded barrels (18,22), which associate as trimers. Ligand-gated protein channels cooperate with a TonB associated inner membrane complex to actively transport ligands via the proton motive force and they form monomeric, (22,24) barrels. The 150-200 N-terminal residues form a plug that blocks the channel from the periplasmic end. The actual alignment was detected with superfamily member TIGR01783: Pssm-ID: 473880 [Multi-domain] Cd Length: 651 Bit Score: 61.66 E-value: 1.75e-10
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Name | Accession | Description | Interval | E-value | |||
TonB-siderophor | TIGR01783 | TonB-dependent siderophore receptor; This subfamily model encompasses a wide variety of ... |
194-310 | 1.75e-10 | |||
TonB-dependent siderophore receptor; This subfamily model encompasses a wide variety of TonB-dependent outer membrane siderophore receptors. It has no overlap with TonB receptors known to transport other substances, but is likely incomplete due to lack of characterizations. It is likely that genuine siderophore receptors will be identified which score below the noise cutoff to this model at which point the model should be updated. [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins] Pssm-ID: 273805 [Multi-domain] Cd Length: 651 Bit Score: 61.66 E-value: 1.75e-10
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TonB_dep_Rec | pfam00593 | TonB dependent receptor; This model now only covers the conserved part of the barrel structure. |
186-309 | 3.73e-08 | |||
TonB dependent receptor; This model now only covers the conserved part of the barrel structure. Pssm-ID: 395474 [Multi-domain] Cd Length: 475 Bit Score: 54.39 E-value: 3.73e-08
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CirA | COG1629 | Outer membrane receptor protein, Fe transport [Inorganic ion transport and metabolism]; |
186-291 | 1.20e-07 | |||
Outer membrane receptor protein, Fe transport [Inorganic ion transport and metabolism]; Pssm-ID: 441236 [Multi-domain] Cd Length: 644 Bit Score: 52.91 E-value: 1.20e-07
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ligand_gated_channel | cd01347 | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ... |
187-310 | 1.26e-06 | |||
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore. Pssm-ID: 238657 [Multi-domain] Cd Length: 635 Bit Score: 49.76 E-value: 1.26e-06
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Name | Accession | Description | Interval | E-value | |||
TonB-siderophor | TIGR01783 | TonB-dependent siderophore receptor; This subfamily model encompasses a wide variety of ... |
194-310 | 1.75e-10 | |||
TonB-dependent siderophore receptor; This subfamily model encompasses a wide variety of TonB-dependent outer membrane siderophore receptors. It has no overlap with TonB receptors known to transport other substances, but is likely incomplete due to lack of characterizations. It is likely that genuine siderophore receptors will be identified which score below the noise cutoff to this model at which point the model should be updated. [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins] Pssm-ID: 273805 [Multi-domain] Cd Length: 651 Bit Score: 61.66 E-value: 1.75e-10
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TonB_dep_Rec | pfam00593 | TonB dependent receptor; This model now only covers the conserved part of the barrel structure. |
186-309 | 3.73e-08 | |||
TonB dependent receptor; This model now only covers the conserved part of the barrel structure. Pssm-ID: 395474 [Multi-domain] Cd Length: 475 Bit Score: 54.39 E-value: 3.73e-08
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CirA | COG1629 | Outer membrane receptor protein, Fe transport [Inorganic ion transport and metabolism]; |
186-291 | 1.20e-07 | |||
Outer membrane receptor protein, Fe transport [Inorganic ion transport and metabolism]; Pssm-ID: 441236 [Multi-domain] Cd Length: 644 Bit Score: 52.91 E-value: 1.20e-07
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ligand_gated_channel | cd01347 | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ... |
187-310 | 1.26e-06 | |||
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore. Pssm-ID: 238657 [Multi-domain] Cd Length: 635 Bit Score: 49.76 E-value: 1.26e-06
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FecA | COG4772 | Outer membrane receptor for Fe3+-dicitrate [Inorganic ion transport and metabolism]; |
191-310 | 3.41e-06 | |||
Outer membrane receptor for Fe3+-dicitrate [Inorganic ion transport and metabolism]; Pssm-ID: 443804 [Multi-domain] Cd Length: 681 Bit Score: 48.39 E-value: 3.41e-06
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Fiu | COG4774 | Outer membrane receptor for monomeric catechols [Inorganic ion transport and metabolism]; |
191-310 | 4.23e-05 | |||
Outer membrane receptor for monomeric catechols [Inorganic ion transport and metabolism]; Pssm-ID: 443806 [Multi-domain] Cd Length: 639 Bit Score: 44.87 E-value: 4.23e-05
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FhuE | COG4773 | Outer membrane receptor for ferric coprogen and ferric-rhodotorulic acid [Inorganic ion ... |
190-310 | 4.81e-04 | |||
Outer membrane receptor for ferric coprogen and ferric-rhodotorulic acid [Inorganic ion transport and metabolism]; Pssm-ID: 443805 [Multi-domain] Cd Length: 692 Bit Score: 41.80 E-value: 4.81e-04
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Blast search parameters | ||||
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