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InterPro: IPR011050 Pectin lyase fold/virulence factor
Protein matches
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UniProtKB Matches: 11341 proteins |
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Accession
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IPR011050 Pectin_lyase_fold/virulence |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR003992 Pertactin virulence factor, N-terminal
IPR012332 Phage P22 tailspike
IPR012334 Pectin lyase fold
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Found in
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IPR000710 Peptidase S6, IgA endopeptidase
IPR017318 Peptidase S8A, subtilisin-related, campylobacter
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Contains
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IPR004899 Pertactin
IPR006626 Parallel beta-helix repeat
IPR006633 Carbohydrate-binding/sugar hydrolysis domain
IPR007742 Periplasmic copper-binding
IPR008638 Filamentous haemagglutinin, N-terminal, bacterial
IPR011459 Protein of unknown function DUF1565
IPR013425 Autotransporter-associated beta strand repeat
IPR013687 Disaggregatase related-2
IPR018040 Pectinesterase, active site
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall [1]. When the backbone of pectin is methylated it is known as pectin and is cleaved by pectin lyase, and when it is demethylated it is known as pectate and is cleaved by pectate lyase. Pectin lyase from Aspergillus niger displays a single-stranded, right-handed parallel beta-helix topology (IPR006626), where each coil contains three beta-strands and three turn regions. Several other virulence factors share this beta-helix topology, although they vary in the number of coils, including bacterial pectate lyases, fungal and bacterial galacturonases (such as rhamnogalacturonase and polygalacturonase), chrondroitinase B from Flavobacterium sp., iota-carrageenase from Alteromonas sp., pectin methylesterase (PemA), P22 tailspike protein from Enterobacteria phage P22, and the virulence factor P.69 pertactin from Bordetella pertussis that mediates adhesion to target mammalian cells [2].
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Structural links
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SCOP:
b.68.1.2
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b.80.1.1
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b.80.1.10
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b.80.1.11
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b.80.1.2
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b.80.1.3
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b.80.1.4
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b.80.1.5
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b.80.1.6
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b.80.1.7
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b.80.1.8
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b.80.1.9
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Additional Reading
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Xiao Z, Bergeron H, Grosse S, Beauchemin M, Garron ML, Shaya D, Sulea T, Cygler M, Lau PC.
Improvement of the thermostability and activity of a pectate lyase by single amino acid substitutions, using a strategy based on melting-temperature-guided sequence alignment.
Appl. Environ. Microbiol. 74 2008 1183-9
[PubMed: 18156340]
http://dx.doi.org/10.1128/AEM.02220-07
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Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D.
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.
Plant Cell 17 2005 849-58
[PubMed: 15722470]
http://dx.doi.org/10.1105/tpc.104.028886
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Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T.
Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49.
J. Mol. Biol. 376 2008 210-20
[PubMed: 18155243]
http://dx.doi.org/10.1016/j.jmb.2007.11.098
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Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW.
Molecular basis of the activity of the phytopathogen pectin methylesterase.
EMBO J. 26 2007 3879-87
[PubMed: 17717531]
http://dx.doi.org/10.1038/sj.emboj.7601816
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Bonivento D, Pontiggia D, Matteo AD, Fernandez-Recio J, Salvi G, Tsernoglou D, Cervone F, Lorenzo GD, Federici L.
Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonase-inhibiting proteins.
Proteins 70 2008 294-9
[PubMed: 17876815]
http://dx.doi.org/10.1002/prot.21610
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InterPro 23.1
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