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The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively . The transglycosylase domain catalyses the polymerisation of murein glycan chains ().
F. Lefevre, M. H. Remy & J. M. Masson; , J Bacteriol 1997;179:4761-4767.: Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. PUBMED:9244263 EPMC:9244263
Di Guilmi AM, Dessen A, Dideberg O, Vernet T; , J Bacteriol 2003;185:4418-4423.: The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains. PUBMED:12867450 EPMC:12867450
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This tab holds annotation information from the InterPro database.
InterPro entry IPR001264
The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates (EC) and related proteins into distinct sequence based families has been described [PUBMED:9334165]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.
The family includes the bifunctional penicillin-binding proteins that have a transglycosylase (N terminus) and transpeptidase (C terminus) domain [PUBMED:9244263] and the monofunctional biosynthetic peptidoglycan transglycosylases [PUBMED:8830253].
|Cellular component||peptidoglycan-based cell wall (GO:0009274)|
|Molecular function||catalytic activity (GO:0003824)|
|Biological process||peptidoglycan biosynthetic process (GO:0009252)|
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Curation and family details
|Seed source:||Pfam-B_558 (release 3.0)|
|Author:||Finn RD, Bateman A|
|Number in seed:||172|
|Number in full:||12887|
|Average length of the domain:||179.10 aa|
|Average identity of full alignment:||35 %|
|Average coverage of the sequence by the domain:||26.43 %|
|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:||17|
|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 Transgly domain has been found. There are 62 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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