Summary: PE family
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This family named after a PE motif near to the amino terminus of the domain. The PE family of proteins all contain an amino-terminal region of about 110 amino acids. The carboxyl terminus of this family are variable and fall into several classes. The largest class of PE proteins is the highly repetitive PGRS class which have a high glycine content. The function of these proteins is uncertain but it has been suggested that they may be related to antigenic variation of Mycobacterium tuberculosis .
Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jage, Nature 1998;393:537-544.: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. PUBMED:9634230 EPMC:9634230
Strong M, Sawaya MR, Wang S, Phillips M, Cascio D, Eisenberg D; , Proc Natl Acad Sci U S A. 2006;103:8060-8065.: Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. PUBMED:16690741 EPMC:16690741
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000084
The human pathogen Mycobacterium tuberculosis harbours a large number of genes that encode proteins whose N-termini contain the characteristic motifs Pro-Glu (PE) or Pro-Pro-Glu (PPE). A subgroup of the PE proteins contains polymorphic GC-rich sequences (PGRS), while a subgroup of the PPE proteins contains major polymorphic tandem repeats (MPTR). The function of most of these proteins remains unknown [PUBMED:19602151]. However, the PE_PGRS proteins from Mycobacterium marinum are secreted by components of the ESX-5 system that belongs to the recently defined type VII secretion systems [PUBMED:18981138]. It has also been reported that the PE_PGRS family of proteins contains multiple calcium-binding and glycine-rich sequence motifs GGXGXD/NXUX. This sequence repeat constitutes a calcium-binding parallel beta-roll or parallel beta-helix structure and is found in RTX toxins secreted by many Gram-negative bacteria [PUBMED:18267304].This family is named after a PE motif near to the amino terminus. The carboxyl terminus of this family are variable and fall into several classes. The largest class of PE proteins is the highly repetitive PGRS class which have a high glycine content. The function of these proteins is uncertain but it has been suggested that they may be related to antigenic variation of Mycobacterium tuberculosis [PUBMED:9634230].
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The WXG100 protein secretion system (Wss) is responsible for the secretion of WXG100 proteins (PF06013), such as ESAT-10 (6 kDa early secreted antigenic target) and CFP-10 (10 kDa culture filtrate protein) in Mycobacterium tuberculosis or EsxA (ESAT-6-like extracellularly secreted protein A) and EsxB in Staphylococcus aureus. These two proteins, generally encoded in the same gene cluster, form a 1:1 heterodimeric complex. These proteins are virulence factors involved in host-pathogen interaction , as demonstrated in Mycobacterium tuberculosis, Staphylococcus aureus or Bacillus anthracis. The Wss is encoded in many other Gram-positive (monoderm) bacteria. This superfamily contains a number of DUFs which are closely related and may or may not represent the same family of proteins.
The clan contains the following 6 members:DUF2563 DUF2580 LXG PE PPE WXG100
We make a range of alignments for each Pfam-A family:
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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Curation and family details
|Seed source:||Pfam-B_253 (release 3.0)|
|Number in seed:||135|
|Number in full:||4012|
|Average length of the domain:||90.80 aa|
|Average identity of full alignment:||46 %|
|Average coverage of the sequence by the domain:||26.20 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 PE domain has been found. There are 2 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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