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
Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in ...
1-199
6.88e-140
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 pfam06316:
Pssm-ID: 473880 [Multi-domain] Cd Length: 199 Bit Score: 388.26 E-value: 6.88e-140
Enterobacterial Ail/Lom protein; This family consists of several bacterial and phage Ail ...
1-199
6.88e-140
Enterobacterial Ail/Lom protein; This family consists of several bacterial and phage Ail/Lom-like proteins. The Yersinia enterocolitica Ail protein is a known virulence factor. Proteins in this family are predicted to consist of eight transmembrane beta-sheets and four cell surface-exposed loops. It is thought that Ail directly promotes invasion and loop 2 contains an active site, perhaps a receptor-binding domain. The phage protein Lom is expressed during lysogeny, and encode host-cell envelope proteins. Lom is found in the bacterial outer membrane, and is homologous to virulence proteins of two other enterobacterial genera. It has been suggested that lysogeny may generally have a role in bacterial survival in animal hosts, and perhaps in pathogenesis.
Pssm-ID: 115004 [Multi-domain] Cd Length: 199 Bit Score: 388.26 E-value: 6.88e-140
Enterobacterial Ail/Lom protein; This family consists of several bacterial and phage Ail ...
1-199
6.88e-140
Enterobacterial Ail/Lom protein; This family consists of several bacterial and phage Ail/Lom-like proteins. The Yersinia enterocolitica Ail protein is a known virulence factor. Proteins in this family are predicted to consist of eight transmembrane beta-sheets and four cell surface-exposed loops. It is thought that Ail directly promotes invasion and loop 2 contains an active site, perhaps a receptor-binding domain. The phage protein Lom is expressed during lysogeny, and encode host-cell envelope proteins. Lom is found in the bacterial outer membrane, and is homologous to virulence proteins of two other enterobacterial genera. It has been suggested that lysogeny may generally have a role in bacterial survival in animal hosts, and perhaps in pathogenesis.
Pssm-ID: 115004 [Multi-domain] Cd Length: 199 Bit Score: 388.26 E-value: 6.88e-140
Outer membrane protein beta-barrel domain; This domain is found in a wide range of outer ...
10-199
3.67e-17
Outer membrane protein beta-barrel domain; This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.
Pssm-ID: 463903 [Multi-domain] Cd Length: 175 Bit Score: 75.13 E-value: 3.67e-17
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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