InterPro : IPR011050

Name  Pectin lyase fold/virulence factor Short Name  Pectin_lyase_fold/virulence
Type  Domain Description  Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall []. 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 nigerdisplays a single-stranded, right-handed parallel beta-helix topology (), 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 pertussisthat mediates adhesion to target mammalian cells [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

3 Child Features

Id Name Short Name Type
IPR012334 Pectin lyase fold Pectin_lyas_fold Domain
IPR022442 Parallel beta-helix repeat-containing domain B-helix_rpt-cont_dom Domain
IPR012332 P22 tailspike C-terminal domain-like P22_tailspike_C-like Domain

11 Contains

Id Name Short Name Type
IPR007742 Periplasmic copper-binding protein NosD, beta helix domain NosD_dom Domain
IPR006626 Parallel beta-helix repeat PbH1 Repeat
IPR022444 Cofactor-binding repeat, putative Cofactor-bd_rpt Repeat
IPR022441 Parallel beta-helix repeat-2 Para_beta_helix_rpt-2 Repeat
IPR011459 Domain of unknown function DUF1565 DUF1565 Domain
IPR013687 Disaggregatase-related Disaggr-rel Domain
IPR006633 Carbohydrate-binding/sugar hydrolysis domain Carb-bd_sugar_hydrolysis-dom Domain
IPR004899 Pertactin, central region Pertactin_central Domain
IPR018040 Pectinesterase, active site Pectinesterase_AS Active_site
IPR013425 Autotransporter-associated beta strand repeat Autotrns_rpt Repeat
IPR008638 Filamentous haemagglutinin, N-terminal Filamn_hemagglutn_N Domain

5 Found In

Id Name Short Name Type
IPR022388 Conserved hypothetical protein CHP03808 CHP03808 Family
IPR003991 Pertactin virulence factor family Pertactin_virulence_factor Family
IPR003992 Pertactin Pertactin Family
IPR017318 Peptidase S8A, subtilisin-related, campylobacter Pept_S8A_subtilisin_campylobac Family
IPR000710 Peptidase S6, IgA endopeptidase Peptidase_S6 Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Jenkins J Structure and evolution of parallel beta-helix proteins. 1998 J Struct Biol 122 236-46
Mayans O Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. 1997 Structure 5 677-89



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)