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10  structures 154  species 1  interaction 217  sequences 3  architectures

Family: LppX_LprAFG (PF07161)

Summary: LppX_LprAFG lipoprotein

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LppX_LprAFG lipoprotein Provide feedback

This entry consists of several lipoproteins mainly from Mycobacterium species, collectively known as the LppX_ LprAFG family. Proteins in this entry include LprG, LppX, LprF and lprA [1, 2, 3, 4, 5, 6].

Literature references

  1. Bigi F, Espitia C, Alito A, Zumarraga M, Romano MI, Cravero S, Cataldi A;, Microbiology. 1997;143:3599-3605.: A novel 27 kDa lipoprotein antigen from Mycobacterium bovis. PUBMED:9387238 EPMC:9387238

  2. Bigi F, Gioffre A, Klepp L, Santangelo MP, Alito A, Caimi K, Meikle V, Zumarraga M, Taboga O, Romano MI, Cataldi A;, Microbes Infect. 2004;6:182-187.: The knockout of the lprG-Rv1410 operon produces strong attenuation of Mycobacterium tuberculosis. PUBMED:14998516 EPMC:14998516

  3. Gehring AJ, Dobos KM, Belisle JT, Harding CV, Boom WH;, J Immunol. 2004;173:2660-2668.: Mycobacterium tuberculosis LprG (Rv1411c): a novel TLR-2 ligand that inhibits human macrophage class II MHC antigen processing. PUBMED:15294983 EPMC:15294983

  4. Sulzenbacher G, Canaan S, Bordat Y, Neyrolles O, Stadthagen G, Roig-Zamboni V, Rauzier J, Maurin D, Laval F, Daffe M, Cambillau C, Gicquel B, Bourne Y, Jackson M;, EMBO J. 2006;25:1436-1444.: LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis. PUBMED:16541102 EPMC:16541102

  5. Steyn AJ, Joseph J, Bloom BR;, Mol Microbiol. 2003;47:1075-1089.: Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD with members of the Lpr family. PUBMED:12581360 EPMC:12581360

  6. Pecora ND, Gehring AJ, Canaday DH, Boom WH, Harding CV;, J Immunol. 2006;177:422-429.: Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function. PUBMED:16785538 EPMC:16785538


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR009830

This entry consists of several lipoproteins mainly from Mycobacterium species, collectively known as the LppX/LprAFG family. Proteins in this entry include:

  • LprG (SWISSPROT) from Mycobacterium tuberculosis: an immunogenic 27 kDa membrane-associated lipoprotein [PUBMED:9387238]. Expression of the LprG protein is essential for the growth of M. tuberculosis in immunocompetent mice [PUBMED:14998516]. Purification of LprG showed that it inhibits MHC-II antigen processing in primary human macrophages, providing a mechanism to avoid the host MHC-II-restricted CD4+ T cell response which is considered essential for control of M. tuberculosis infection [PUBMED:15294983].
  • LppX: a lipoprotein required for the translocation of complex lipids to the outer membrane of Mycobacterium tuberculosis. Its structure consists of a U-shaped beta-half-barrel with a large hydrophobic cavity [PUBMED:16541102].
  • LprF: a membrane lipoprotein involved in the kdp signal transduction pathway, thought to be the primary response to osmotic stress [PUBMED:12581360].
  • lprA: a lipoprotein agonist of TLR2 that regulates innate immunity and APC function [PUBMED:16785538].

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 LolA_LolB (CL0048), which has the following description:

Gram-negative bacteria lipoproteins are anchored to the periplasmic surface of the inner or outer membrane depending on the sorting signal, which is the residue at position 2 of the polypeptide. Five Lol proteins are involved in the sorting and membrane localisation of lipoprotein. An ATP-binding cassette (ABC) transporter, LolCDE, releases outer membrane-specific lipoproteins from the inner membrane, causing the formation of a complex between the released lipoproteins and the periplasmic molecular chaperone LolA. When this complex interacts with outer membrane receptor LolB, the lipoproteins are transferred from LolA to LolB and then localised to the outer membrane. The structures of LolA and LolB are remarkably similar to each other. Both have a hydrophobic cavity consisting of an unclosed beta-barrel and an alpha-helical lid [1,2].

The clan contains the following 15 members:

DUF1329 DUF1571 DUF2092 DUF3108 DUF3261 DUF4292 DUF4412 DUF576 LolA LolA_2 LolA_like LolB LppX_LprAFG MucB_RseB Porph_ging

Alignments

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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics 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.

  Seed
(14)
Full
(217)
Representative proteomes UniProt
(719)
NCBI
(1312)
Meta
(1)
RP15
(34)
RP35
(107)
RP55
(228)
RP75
(375)
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PP/heatmap 1 View               

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

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

Format an alignment

  Seed
(14)
Full
(217)
Representative proteomes UniProt
(719)
NCBI
(1312)
Meta
(1)
RP15
(34)
RP35
(107)
RP55
(228)
RP75
(375)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

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.

  Seed
(14)
Full
(217)
Representative proteomes UniProt
(719)
NCBI
(1312)
Meta
(1)
RP15
(34)
RP35
(107)
RP55
(228)
RP75
(375)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

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...

Trees

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: Pfam-B_16343 (release 10.0)
Previous IDs: DUF1396; PF07161;
Type: Family
Author: Moxon SJ
Number in seed: 14
Number in full: 217
Average length of the domain: 190.90 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 76.98 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.0 24.0
Trusted cut-off 24.0 24.0
Noise cut-off 23.8 23.9
Model length: 192
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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

Selections

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Interactions

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

LppX_LprAFG

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 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 LppX_LprAFG domain has been found. There are 10 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 seqence.

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