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20  structures 332  species 1  interaction 366  sequences 15  architectures

Clan: OML_zippers (CL0590)

Summary

Major outer membrane lipoprotein zipper superfamily Add an annotation

This is a superfamily of short outer membrane lipoporteins that are coiled-coils of alpha-helices. The families included are both leucine and alanine zippers. A zipper motif is a heptad or seven-residue repeat, represented by X..X...X..X...X..X...X..X...X..X, etc, where the X is hydrophobic residue, usually a leucine or alanine, and the intermediate residues are largely polar or hydrophilic; that is, the responsible residues occur at positions 1 and 4 in the heptad. Monomers combine together into dimers and higher order structures. Coiled-coil motifs are ubiquitous mediators of specific protein-protein interactions, in this case outer membrane 'tubes', by forming interlocking hydrophobic seams between the alpha-helical chains [1].

This clan contains 2 families and the total number of domains in the clan is 366. The clan was built by P Coggill.

Literature references

  1. Abarca F, Gutierrez-Maldonado SE, Parada P, Martinez P, Maass A, Perez-Acle T;, PeerJ. 2014;2:e457.: Insights on the structure and stability of Licanantase: a trimeric acid-stable coiled-coil lipoprotein from Acidithiobacillus thiooxidans. PUBMED:25165619 EPMC:25165619

Members

This clan contains the following 2 member families:

Alanine_zipper LPP

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
Alanine_zipper (PF11839) 197 (53.8%) View
LPP (PF04728) 169 (46.2%) View
Total: 2 Total: 366 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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Interactions

There is 1 interaction for this clan. More...

Interacting families
A B
LPP LPP

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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