Summary: Oligogalacturonate-specific porin protein (KdgM)
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Oligogalacturonate-specific porin protein (KdgM) Provide feedback
This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM (Q934G3) 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 .
Blot N, Berrier C, Hugouvieux-Cotte-Pattat N, Ghazi A, Condemine G; , J Biol Chem 2002;277:7936-7944.: The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family. PUBMED:11773048 EPMC:11773048
External database links
|Transporter classification:||1.B.21 1.B.35|
This tab holds annotation information from the InterPro database.
InterPro entry IPR009331
This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM (SWISSPROT) from Erwinia chrysanthemi. The phytopathogenic Gram-negative bacteria E. 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 [PUBMED:11773048].
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Curation and family details
|Seed source:||Pfam-B_10852 (release 9.0)|
|Number in seed:||7|
|Number in full:||1133|
|Average length of the domain:||209.70 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||93.83 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the KdgM domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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