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InterPro: IPR003343 Bacterial Ig-like, group 2

Protein matchesHelp
UniProtKB
Matches:
1734 proteins
AccessionHelp IPR003343 Big_2
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR003535 Intimin bacterial adhesion mediator protein
IPR008964 Invasin/intimin cell-adhesion
IPR017312 Peptidase S8A, subtilisin-related, shewanella-2
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Proteins that contain this domain are found in a variety of bacterial and phage surface proteins such as intimins. Intimin is a bacterial cell-adhesion molecule that mediates the intimate bacterial host-cell interaction. It contains three domains; two immunoglobulin-like domains and a C-type lectin-like module implying that carbohydrate recognition may be important in intimin-mediated cell adhesion [1].

Structural linksHelp
SCOP: b.1.14.1
CATH: 2.60.40.1080
Database linksHelp
PANDIT: PF02368
Blocks: IPB003343
Pfam Clan: CL0159.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003343 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P03733 Major tail protein V

P11654 Nuclear pore membrane glycoprotein 210

P19809 Intimin

Q5VU65 Nuclear pore membrane glycoprotein 210-like

Q9D2F7 Nuclear pore membrane glycoprotein 210-like

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003535 Intimin bacterial adhesion mediator protein
IPR016187 C-type lectin fold
IPR016186 C-type lectin-like
IPR008964 Invasin/intimin cell-adhesion
IPR003343 Bacterial Ig-like, group 2
IPR013117 Intimin, C-terminal
IPR003344 Bacterial Ig-like, group 1
IPR002482 Peptidoglycan-binding Lysin subgroup
IPR018392 Peptidoglycan-binding lysin domain
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Kelly G, Prasannan S, Daniell S, Fleming K, Frankel G, Dougan G, Connerton I, Matthews S.
Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli.
Nat. Struct. Biol. 6 313-8 1999 [PubMed: 10201396]
http://dx.doi.org/10.1038/7545

Additional ReadingHelp
Luo Y, Frey EA, Pfuetzner RA, Creagh AL, Knoechel DG, Haynes CA, Finlay BB, Strynadka NC.
Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.
Nature 405 2000 1073-7 [PubMed: 10890451]
http://dx.doi.org/10.1038/35016618
Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S.
Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli.
EMBO J. 19 2000 2452-64 [PubMed: 10835344]
http://dx.doi.org/10.1093/emboj/19.11.2452
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InterPro 23.1