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Conserved domains on  [gi|1691303092|ref|WP_139787403|]
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carbohydrate porin, partial [Klebsiella pneumoniae]

Protein Classification

porin family protein( domain architecture ID 229388)

porin family protein is a member of a large superfamily consisting of classical (gram-negative ) porins which are non-specific channels for small hydrophillic molecules, maltoporin-like channels which have specificities for various sugars, and ligand-gated protein channels which cooperate with a TonB associated inner membrane complex to actively transport ligands via the proton motive force

Graphical summary

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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 ...
 11-105 6.28e-31

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 pfam02264:

Pssm-ID: 473880  Cd Length: 385  Bit Score: 112.01  E-value: 6.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNESNG-GEFQISKAFKSAQGAIWDLNVMFDHWSDE--------VNLKKAYVGVTNVLESNPNAYIWAGRD 81
Cdd:pfam02264  23 GGAGGKYRLGNECDTyGELQLGKELTKEDGAKFKFDVMLAYSSSGsndwegtdFNLRQAYVEASNLLPFLPEATLWAGKR 102

                          90       100
                  ....*....|....*....|....
gi 1691303092  82 FHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:pfam02264 103 FYRRNDIHINDFYYWDLSGTGAGV 126
 
Name Accession Description Interval E-value
LamB pfam02264
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
 11-105 6.28e-31

LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.


Pssm-ID: 426687  Cd Length: 385  Bit Score: 112.01  E-value: 6.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNESNG-GEFQISKAFKSAQGAIWDLNVMFDHWSDE--------VNLKKAYVGVTNVLESNPNAYIWAGRD 81
Cdd:pfam02264  23 GGAGGKYRLGNECDTyGELQLGKELTKEDGAKFKFDVMLAYSSSGsndwegtdFNLRQAYVEASNLLPFLPEATLWAGKR 102

                          90       100
                  ....*....|....*....|....
gi 1691303092  82 FHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:pfam02264 103 FYRRNDIHINDFYYWDLSGTGAGV 126
Maltoporin-like cd01346
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
 12-105 4.82e-19

The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the diffusion of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an 18-strand antiparallel beta-barrel (18,22). Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllular side, while short turns are in the periplasm.Tightly-bound water molecules are found in the eyelet of the passage, and only substrates that can displace and replace the broken hydrogen bonds are likely to enter the pore. In the MPR structure, loops 4,6, and 9 have the greatest mobility and are highly variable; these are postulated to attract maltodextrins.


Pssm-ID: 238656  Cd Length: 392  Bit Score: 80.11  E-value: 4.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  12 GASAIGRLGNESNG-GEFQISKAFKSAQGAIWDLNVMFDHWSDE------------VNLKKAYVGVTNVLESNPNAYIWA 78
Cdd:cd01346    27 GGGSVGRLGNECDTyFELGLKKEVYNDNGVTADFVVMVAQGNGQsndwtfaaddgdLNVRQAYVELKGLLPFLPGATFWA 106

                          90       100
                  ....*....|....*....|....*..
gi 1691303092  79 GRDFHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:cd01346   107 GKRFYRRHDIHILDFYYWNTSGTGAGI 133
LamB COG4580
Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];
11-105 3.37e-18

Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];


Pssm-ID: 443637  Cd Length: 408  Bit Score: 77.66  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNES-NGGEFQISKAFKSAQGAIWDLNVMFDHWSD-------------EVNLKKAYVGVTNVLESNPNAYI 76
Cdd:COG4580    50 PGAGSKYRLGNECdTYAELGLGQELYKEDGKTFYVDSMLAYSNDqsndwestngddgDFALRQAYVQAKGLIPALPGATF 129

                          90       100
                  ....*....|....*....|....*....
gi 1691303092  77 WAGRDFHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:COG4580   130 WAGKRYYQRHDVHINDFYYWNISGPGAGI 158
lamB PRK09360
maltoporin LamB;
11-105 3.76e-11

maltoporin LamB;


Pssm-ID: 236481  Cd Length: 415  Bit Score: 57.69  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNES-NGGEFQISKAFKSAQGAIWDLNVMFDHWSDEVN--------LKKAYVGVTNVLESNPNAYIWAGRD 81
Cdd:PRK09360   51 TGAQSKYRLGNECeTYAELKLGQELWKEGDKSFYFDSMVAYSVNQQNdwestdpaLREFNVQAKNLIEWLPGATLWAGKR 130

                          90       100
                  ....*....|....*....|....
gi 1691303092  82 FHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:PRK09360  131 FYQRHDVHMIDFYYWDISGPGAGI 154
 
Name Accession Description Interval E-value
LamB pfam02264
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
 11-105 6.28e-31

LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.


Pssm-ID: 426687  Cd Length: 385  Bit Score: 112.01  E-value: 6.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNESNG-GEFQISKAFKSAQGAIWDLNVMFDHWSDE--------VNLKKAYVGVTNVLESNPNAYIWAGRD 81
Cdd:pfam02264  23 GGAGGKYRLGNECDTyGELQLGKELTKEDGAKFKFDVMLAYSSSGsndwegtdFNLRQAYVEASNLLPFLPEATLWAGKR 102

                          90       100
                  ....*....|....*....|....
gi 1691303092  82 FHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:pfam02264 103 FYRRNDIHINDFYYWDLSGTGAGV 126
Maltoporin-like cd01346
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
 12-105 4.82e-19

The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the diffusion of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an 18-strand antiparallel beta-barrel (18,22). Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllular side, while short turns are in the periplasm.Tightly-bound water molecules are found in the eyelet of the passage, and only substrates that can displace and replace the broken hydrogen bonds are likely to enter the pore. In the MPR structure, loops 4,6, and 9 have the greatest mobility and are highly variable; these are postulated to attract maltodextrins.


Pssm-ID: 238656  Cd Length: 392  Bit Score: 80.11  E-value: 4.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  12 GASAIGRLGNESNG-GEFQISKAFKSAQGAIWDLNVMFDHWSDE------------VNLKKAYVGVTNVLESNPNAYIWA 78
Cdd:cd01346    27 GGGSVGRLGNECDTyFELGLKKEVYNDNGVTADFVVMVAQGNGQsndwtfaaddgdLNVRQAYVELKGLLPFLPGATFWA 106

                          90       100
                  ....*....|....*....|....*..
gi 1691303092  79 GRDFHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:cd01346   107 GKRFYRRHDIHILDFYYWNTSGTGAGI 133
LamB COG4580
Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];
11-105 3.37e-18

Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];


Pssm-ID: 443637  Cd Length: 408  Bit Score: 77.66  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNES-NGGEFQISKAFKSAQGAIWDLNVMFDHWSD-------------EVNLKKAYVGVTNVLESNPNAYI 76
Cdd:COG4580    50 PGAGSKYRLGNECdTYAELGLGQELYKEDGKTFYVDSMLAYSNDqsndwestngddgDFALRQAYVQAKGLIPALPGATF 129

                          90       100
                  ....*....|....*....|....*....
gi 1691303092  77 WAGRDFHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:COG4580   130 WAGKRYYQRHDVHINDFYYWNISGPGAGI 158
lamB PRK09360
maltoporin LamB;
11-105 3.76e-11

maltoporin LamB;


Pssm-ID: 236481  Cd Length: 415  Bit Score: 57.69  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  11 NGASAIGRLGNES-NGGEFQISKAFKSAQGAIWDLNVMFDHWSDEVN--------LKKAYVGVTNVLESNPNAYIWAGRD 81
Cdd:PRK09360   51 TGAQSKYRLGNECeTYAELKLGQELWKEGDKSFYFDSMVAYSVNQQNdwestdpaLREFNVQAKNLIEWLPGATLWAGKR 130

                          90       100
                  ....*....|....*....|....
gi 1691303092  82 FHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:PRK09360  131 FYQRHDVHMIDFYYWDISGPGAGI 154
PRK12395 PRK12395
maltoporin; Provisional
 16-105 2.88e-04

maltoporin; Provisional


Pssm-ID: 183498  Cd Length: 419  Bit Score: 38.40  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691303092  16 IGRLGNESNG-GEFQISKAFKSAQGAIWDLNVMFDHWSDEVN-------------LKKAYVGVTNVLESNPNAYIWAGRD 81
Cdd:PRK12395   53 VGRLGNESDTyGEIGLGAEVYKKEDVSFYLDSMVSMLSDGSNdsettigddaqfgLRQLNLQIKGLIPGDKEAVIWGGKR 132

                          90       100
                  ....*....|....*....|....
gi 1691303092  82 FHQRPQQGINDYFWMNHDGQGAGV 105
Cdd:PRK12395  133 YYQRHDLHIIDTKYWNISGSGAGI 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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