Summary: Cleaved Adhesin Domain
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Cleaved Adhesin Domain Provide feedback
This is a family of bacterial protein modules thought to function in various roles including cell adhesion, cell lysis and carbohydrate binding . A tandem repeat of these modules (either two or three repeats) constitute the haemagglutinin/adhesin (HA) regions of the gingipains, RgpA, Q51816 and Kgp, P72194 and P72197  expressed by Porphyromonas gingivalis (Bacteroides gingivalis) . They form components of the major extracellular virulence complex RgpA-Kgp - a mixture of proteinases and adhesin domains . The adhesin domains in this complex are found in proteinase-cleaved forms when isolated from the cell surface . Haemagglutinin genes of P. gingivalis  (hagA1 HAGA1_PORGI - P59915 - and hagA2 HAGA2_PORGI - Q51845) suggest that such proteins are composed of eight to ten tandem repeats of these adhesin modules . Genomic data predicts that homologous protein modules are also expressed by a number of other bacteria and form part of putative multi-domain proteins, eg. Q26BR9 and B0VGL6. These domains may be acting in concert with other adhesion modules thought to be part of these multi-domain proteins such as fibronectin type III, PF00041 and Meprin, A5, mu (MAM), PF00629 domains.
Li N, Yun P, Nadkarni MA, Ghadikolaee NB, Nguyen KA, Lee M, Hunter N, Collyer CA;, Mol Microbiol. 2010; [Epub ahead of print]: STRUCTURE DETERMINATION AND ANALYSIS OF A HEMOLYTIC GINGIPAIN ADHESIN DOMAIN FROM PORPHYROMONAS GINGIVALIS. PUBMED:20233299 EPMC:20233299
Pavloff N, Potempa J, Pike RN, Prochazka V, Kiefer MC, Travis J, Barr PJ;, J Biol Chem. 1995;270:1007-1010.: Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein. PUBMED:7836351 EPMC:7836351
Pavloff N, Pemberton PA, Potempa J, Chen WC, Pike RN, Prochazka V, Kiefer MC, Travis J, Barr PJ;, J Biol Chem. 1997;272:1595-1600.: Molecular cloning and characterization of Porphyromonas gingivalis lysine-specific gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases. PUBMED:8999833 EPMC:8999833
Bhogal PS, Slakeski N, Reynolds EC; , Microbiology 1997;143:2485-2495.: A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins. PUBMED:9245829 EPMC:9245829
Veith PD, Talbo GH, Slakeski N, Dashper SG, Moore C, Paolini RA, Reynolds EC;, Biochem J. 2002;363:105-115.: Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50. PUBMED:11903053 EPMC:11903053
Han N, Whitlock J, Progulske-Fox A;, Infect Immun. 1996;64:4000-4007.: The hemagglutinin gene A (hagA) of Porphyromonas gingivalis 381 contains four large, contiguous, direct repeats. PUBMED:8926061 EPMC:8926061
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011628
This conserved region is found in a group of haemagglutinins and peptidases, e.g. INTERPRO, that, in Porphyromonas gingivalis (Bacteroides gingivalis), form components of the major extracellular virulence complex RgpA-Kgp - a mixture of proteinases and adhesins [PUBMED:10858222]. These domains are cleaved from the original polyprotein and form part of the adhesins [PUBMED:9245829].
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This superfamily includes a diverse range of carbohydrate binding domains and glycosyl hydrolase enzymes that share a common structure.
The clan contains the following 18 members:Cleaved_Adhesin DUF1080 DUF2401 Gal-bind_lectin Glyco_hydro_11 Glyco_hydro_12 Glyco_hydro_16 Glyco_hydro_7 Laminin_G_1 Laminin_G_2 Laminin_G_3 Lectin_leg-like Lectin_legB MAM Pentaxin Sialidase SKN1 Toxin_R_bind_N
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Yeats C|
|Author:||Yeats C, Collyer C|
|Number in seed:||4|
|Number in full:||353|
|Average length of the domain:||148.30 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||23.20 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|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 Cleaved_Adhesin domain has been found. There are 7 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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