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Conserved domains on  [gi|1452939835|emb|SWW94879|]
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outer membrane receptor FepA [Klebsiella pneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13528 super family cl36255
outer membrane receptor FepA; Provisional
 10-75 1.17e-25

outer membrane receptor FepA; Provisional


The actual alignment was detected with superfamily member PRK13528:

Pssm-ID: 237413 [Multi-domain]  Cd Length: 727  Bit Score: 98.68  E-value: 1.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452939835  10 TRREDTCGLSGKELGAYSPVETNFNYDSNKILRLNVCVSNILDKQIYRFSEGASPYNELGWAYYVG 75
Cdd:PRK13528  657 SRSEETGGLSGKELGAYSLVGVNVNYDINKNLRLNVGVSNLFDKQIYREGEGANTYNEPGRAYYAG 722
 
Name Accession Description Interval E-value
PRK13528 PRK13528
outer membrane receptor FepA; Provisional
 10-75 1.17e-25

outer membrane receptor FepA; Provisional


Pssm-ID: 237413 [Multi-domain]  Cd Length: 727  Bit Score: 98.68  E-value: 1.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452939835  10 TRREDTCGLSGKELGAYSPVETNFNYDSNKILRLNVCVSNILDKQIYRFSEGASPYNELGWAYYVG 75
Cdd:PRK13528  657 SRSEETGGLSGKELGAYSLVGVNVNYDINKNLRLNVGVSNLFDKQIYREGEGANTYNEPGRAYYAG 722
ligand_gated_channel cd01347
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ...
 12-75 2.33e-03

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: 35.12  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1452939835  12 REDTCGLSGKELGAYSPVETNFNYDSNKILRLNVCVSNILDKQIYRF----SEGASPYNELGWAYYVG 75
Cdd:cd01347   563 ADTANGNNTVKVPGYTLVDLSASYQFTKNLTLRLGVNNLFDKDYYTSlsvrGSGLYGYYGPGRTYYLS 630
 
Name Accession Description Interval E-value
PRK13528 PRK13528
outer membrane receptor FepA; Provisional
 10-75 1.17e-25

outer membrane receptor FepA; Provisional


Pssm-ID: 237413 [Multi-domain]  Cd Length: 727  Bit Score: 98.68  E-value: 1.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452939835  10 TRREDTCGLSGKELGAYSPVETNFNYDSNKILRLNVCVSNILDKQIYRFSEGASPYNELGWAYYVG 75
Cdd:PRK13528  657 SRSEETGGLSGKELGAYSLVGVNVNYDINKNLRLNVGVSNLFDKQIYREGEGANTYNEPGRAYYAG 722
PRK13524 PRK13524
FepA family TonB-dependent siderophore receptor;
13-75 1.17e-07

FepA family TonB-dependent siderophore receptor;


Pssm-ID: 237410 [Multi-domain]  Cd Length: 744  Bit Score: 47.33  E-value: 1.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1452939835  13 EDTCGLSGKELGAYSPVETNFNYDSNKILRLNVCVSNILDKQIYR-----------FSEGASPYNELGWAYYVG 75
Cdd:PRK13524  666 QPVTGSATKEVSPYSIVGLSATYDVTKNVSLTGGVDNLFDKRLWRegnaqttgdliAGAGAYTYNEPGRTYYMS 739
ligand_gated_channel cd01347
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ...
 12-75 2.33e-03

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: 35.12  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1452939835  12 REDTCGLSGKELGAYSPVETNFNYDSNKILRLNVCVSNILDKQIYRF----SEGASPYNELGWAYYVG 75
Cdd:cd01347   563 ADTANGNNTVKVPGYTLVDLSASYQFTKNLTLRLGVNNLFDKDYYTSlsvrGSGLYGYYGPGRTYYLS 630
 
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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