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 ...
49-169
7.62e-45
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 pfam02462:
Pssm-ID: 473880 [Multi-domain] Cd Length: 126 Bit Score: 143.81 E-value: 7.62e-45
Opacity family porin protein; Pathogenic Neisseria spp. possess a repertoire of phase-variable ...
49-169
7.62e-45
Opacity family porin protein; Pathogenic Neisseria spp. possess a repertoire of phase-variable Opacity proteins that mediate various pathogen--host cell interactions. These proteins are integral membrane proteins related to other porins.
Pssm-ID: 308205 [Multi-domain] Cd Length: 126 Bit Score: 143.81 E-value: 7.62e-45
Opacity family porin protein; Pathogenic Neisseria spp. possess a repertoire of phase-variable ...
49-169
7.62e-45
Opacity family porin protein; Pathogenic Neisseria spp. possess a repertoire of phase-variable Opacity proteins that mediate various pathogen--host cell interactions. These proteins are integral membrane proteins related to other porins.
Pssm-ID: 308205 [Multi-domain] Cd Length: 126 Bit Score: 143.81 E-value: 7.62e-45
Outer membrane protein beta-barrel domain; This domain is found in a wide range of outer ...
21-169
6.50e-11
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: 57.79 E-value: 6.50e-11
OmpW family; This family includes outer membrane protein W (OmpW) proteins from a variety of ...
70-169
3.42e-03
OmpW family; This family includes outer membrane protein W (OmpW) proteins from a variety of bacterial species. This protein may form the receptor for S4 colicins in E. coli.
Pssm-ID: 397830 Cd Length: 193 Bit Score: 36.67 E-value: 3.42e-03
MltA-interacting protein MipA; This family consists of several bacterial MltA-interacting ...
112-169
6.62e-03
MltA-interacting protein MipA; This family consists of several bacterial MltA-interacting protein (MipA) like sequences. As well as interacting with the membrane-bound lytic transglycosylase MltA, MipA is known to bind to PBP1B, a bifunctional murein transglycosylase/transpeptidase. MipA is considered to be a structural protein mediating the assembly of MltA to PBP1B into a complex.
Pssm-ID: 461968 Cd Length: 221 Bit Score: 35.83 E-value: 6.62e-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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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