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24  structures 235  species 0  interactions 274  sequences 2  architectures

Family: LPP (PF04728)

Summary: Lipoprotein leucine-zipper

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Braun's lipoprotein". More...

Braun's lipoprotein Edit Wikipedia article

Most abundant membrane protein. Bound by the covalent bond to the peptidoglycan layer and embedded in the outer membrane by its hydrophobic head. Tightly links the outer membrane and the peptidoglycan layer.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Lipoprotein leucine-zipper Provide feedback

This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes.

Literature references

  1. Shu W, Liu J, Ji H, Lu M;, J Mol Biol. 2000;299:1101-1112.: Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution. PUBMED:10843861 EPMC:10843861

  2. Liu J, Cao W, Lu M;, J Mol Biol. 2002;318:877-888.: Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. PUBMED:12054830 EPMC:12054830

  3. Liu J, Dai J, Lu M;, Biochemistry. 2003;42:5657-5664.: Zinc-mediated helix capping in a triple-helical protein. PUBMED:12741822 EPMC:12741822

  4. Liu J, Yong W, Deng Y, Kallenbach NR, Lu M;, Proc Natl Acad Sci U S A. 2004;101:16156-16161.: Atomic structure of a tryptophan-zipper pentamer. PUBMED:15520380 EPMC:15520380

  5. Liu J, Zheng Q, Deng Y, Kallenbach NR, Lu M;, J Mol Biol. 2006;361:168-179.: Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction. PUBMED:16828114 EPMC:16828114

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006817

This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP [ PUBMED:10843861 ]. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes [ PUBMED:12054830 , PUBMED:15520380 , PUBMED:16828114 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan OML_zippers (CL0590), which has the following description:

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].

The clan contains the following 3 members:

Alanine_zipper FadA LPP


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: DOMO:DM04880;
Previous IDs: none
Type: Coiled-coil
Sequence Ontology: SO:0001080
Author: Kerrison ND , Coggill P
Number in seed: 12
Number in full: 274
Average length of the domain: 53.5 aa
Average identity of full alignment: 50 %
Average coverage of the sequence by the domain: 47.01 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 29.1 29.1
Trusted cut-off 29.1 29.3
Noise cut-off 29.0 28.8
Model length: 53
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


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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 LPP domain has been found. There are 24 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 sequence.

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