Summary: D-ala-D-ala dipeptidase
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D-ala-D-ala dipeptidase Provide feedback
No Pfam abstract.
Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH; , Mol Cell 1998;2:75-84.: The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. PUBMED:9702193 EPMC:9702193
Internal database links
|SCOOP:||VanY Med6 Peptidase_M15_4|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000755
This group of metallopeptidases belong to MEROPS peptidase family M15 (clan MD), subfamily M15D (vanX D-Ala-D-Ala dipeptidase).
The D-alanyl-D-alanine dipeptidase enzyme from Enterococcus faecalis is also known as the vancomycin resistance protein VanX, and hydrolyses D-ala-D-ala. It has a 250-fold differential in catalytic efficiency for hydrolysis of D-ala-D-ala versus D-ala-D-lactate. The latter therefore remains intact for subsequent incorporation into peptidoglycan precursors that terminate in the dipeptide D-ala-D-lactate rather than the dipeptide D-ala-D-ala, thereby preventing vancomycin from binding. The enzyme requires a metal cofactor, and is induced by vancomycin through regulation by VanS and VanR.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cell wall (GO:0005618)|
|Molecular function||metallopeptidase activity (GO:0008237)|
|dipeptidase activity (GO:0016805)|
|Biological process||proteolysis (GO:0006508)|
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This clan is comprised of carboxypeptidases and the N-terminal domain from Sonic hedgehog proteins. The structure of the latter is similar to the peptidases, but the N-terminal domain of hedgehog has been demonstrate not to be involved in peptidase activity, but is more likely involved in signal transduction .
The clan contains the following 7 members:HH_signal Peptidase_M15 Peptidase_M15_2 Peptidase_M15_3 Peptidase_M15_4 Peptidase_M74 VanY
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Curation and family details
|Seed source:||Psiblast Q47749|
|Number in seed:||4|
|Number in full:||517|
|Average length of the domain:||172.50 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||75.39 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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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 Peptidase_M15 domain has been found. There are 6 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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