carbohydrate porin belonging to the LamB family whose members are thought to bind various sugars; similar to maltoporin which is involved in the transport of maltose and maltodextrins
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
117-550
3.59e-103
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: 315.78 E-value: 3.59e-103
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, ...
21-51
3.10e-05
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, N-terminal extension of the outer membrane maltoporins, pfam02264, LamB.
:
Pssm-ID: 431901 Cd Length: 31 Bit Score: 41.09 E-value: 3.10e-05
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
117-550
3.59e-103
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: 315.78 E-value: 3.59e-103
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
113-550
9.62e-76
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: 244.98 E-value: 9.62e-76
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, ...
21-51
3.10e-05
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, N-terminal extension of the outer membrane maltoporins, pfam02264, LamB.
Pssm-ID: 431901 Cd Length: 31 Bit Score: 41.09 E-value: 3.10e-05
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-90
2.99e-03
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 2.99e-03
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
117-550
3.59e-103
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: 315.78 E-value: 3.59e-103
The Maltoporin-like channels (LamB porin) form a trimeric structure which facilitate the ...
113-550
9.62e-76
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: 244.98 E-value: 9.62e-76
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, ...
21-51
3.10e-05
Maltoporin periplasmic N-terminal extension; This domain would appear to be the periplasmic, N-terminal extension of the outer membrane maltoporins, pfam02264, LamB.
Pssm-ID: 431901 Cd Length: 31 Bit Score: 41.09 E-value: 3.10e-05
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-90
2.99e-03
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 2.99e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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