Oligogalacturonate-specific porin protein KdgM [Klebsiella quasipneumoniae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| KdgM super family | cl11629 | Oligogalacturonate-specific porin protein (KdgM); This family consists of several bacterial ... |
11-215 | 1.75e-29 | ||||
Oligogalacturonate-specific porin protein (KdgM); This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM from Erwinia chrysanthemi. The phytopathogenic Gram-negative bacteria Erwinia chrysanthemi secretes pectinases, which are able to degrade the pectic polymers of plant cell walls, and uses the degradation products as a carbon source for growth. KdgM is a major outer membrane protein, whose synthesis is strongly induced in the presence of pectic derivatives. KdgM behaves like a voltage-dependent porin that is slightly selective for anions and that exhibits fast block in the presence of trigalacturonate. In contrast to most porins, KdgM seems to be monomeric. The actual alignment was detected with superfamily member pfam06178: Pssm-ID: 416341 Cd Length: 215 Bit Score: 109.18 E-value: 1.75e-29
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| Name | Accession | Description | Interval | E-value | ||||
| KdgM | pfam06178 | Oligogalacturonate-specific porin protein (KdgM); This family consists of several bacterial ... |
11-215 | 1.75e-29 | ||||
Oligogalacturonate-specific porin protein (KdgM); This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM from Erwinia chrysanthemi. The phytopathogenic Gram-negative bacteria Erwinia chrysanthemi secretes pectinases, which are able to degrade the pectic polymers of plant cell walls, and uses the degradation products as a carbon source for growth. KdgM is a major outer membrane protein, whose synthesis is strongly induced in the presence of pectic derivatives. KdgM behaves like a voltage-dependent porin that is slightly selective for anions and that exhibits fast block in the presence of trigalacturonate. In contrast to most porins, KdgM seems to be monomeric. Pssm-ID: 399289 Cd Length: 215 Bit Score: 109.18 E-value: 1.75e-29
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| gram_neg_porins | cd00342 | Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ... |
110-215 | 4.05e-03 | ||||
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus. Pssm-ID: 238208 [Multi-domain] Cd Length: 329 Bit Score: 37.35 E-value: 4.05e-03
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| Name | Accession | Description | Interval | E-value | ||||
| KdgM | pfam06178 | Oligogalacturonate-specific porin protein (KdgM); This family consists of several bacterial ... |
11-215 | 1.75e-29 | ||||
Oligogalacturonate-specific porin protein (KdgM); This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM from Erwinia chrysanthemi. The phytopathogenic Gram-negative bacteria Erwinia chrysanthemi secretes pectinases, which are able to degrade the pectic polymers of plant cell walls, and uses the degradation products as a carbon source for growth. KdgM is a major outer membrane protein, whose synthesis is strongly induced in the presence of pectic derivatives. KdgM behaves like a voltage-dependent porin that is slightly selective for anions and that exhibits fast block in the presence of trigalacturonate. In contrast to most porins, KdgM seems to be monomeric. Pssm-ID: 399289 Cd Length: 215 Bit Score: 109.18 E-value: 1.75e-29
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| gram_neg_porins | cd00342 | Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ... |
110-215 | 4.05e-03 | ||||
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus. Pssm-ID: 238208 [Multi-domain] Cd Length: 329 Bit Score: 37.35 E-value: 4.05e-03
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