Mol. Microbiol.

We have determined the nucleotide sequences of the genes encoding the fimbrial subunits representative of the known Bacteroides nodosus serogroups. All of the genes are preceded by a highly conserved region which includes the likely promoter and transcriptional regulator sites as well as the ribosome-biding site, and are followed within a short but variable distance by a sequence with the characteristics of a transcription termination or attenuation signal. Based on sequence and organization, the subunits can be divided into two major classes called I (serogroups A, B, C, E, F, G, and I) and II (serogroups D and H). All contain the same seven-amino-acid positively charged leader sequence and conserved hydrophobic amino-terminal sequence typical of type 4 fibriae. Beyond this point the class II subunits are quite different from class I and share features more in common with those from other type 4 fimbriate bacteria, such as Moraxella bovis and Pseudomonas aeruginosa. The larger class I may be further subdivided into two subsets: (i) [A, E, F)(B, I)) and (ii) (C, G). These proteins exhibit three major clusters of variation, at either end of the presumptive disulphide loop which spans the central third of the protein, and near the carboxy-terimus, with dispersed changes in between. The length of the mature subunits varies from 152-156 amino acids, and the variation includes small insertions or deletions in the variable clusters between more conserved domains. The class II subunits are 149 amino acids in length and contain two pairs of cysteine residues: one is at the end of the amino-terminal conserved region, and the other is at the end of the protein. The major variation occurs in the central region of the molecule, and again small insertions or deletions are required to align adjacent conserved domains. There is also a striking absence of silent codon changes in the 5' coding region of all of these genes, indicating that these sequences have a secondary genetic function, probably in recombinational exchange.

Source:http://purl.uniprot.org/citations/1675419

Statements in which the resource exists.
SubjectPredicateObjectContext
http://purl.uniprot.org/cit...rdf:typeuniprot:Journal_Citationlld:uniprot
http://purl.uniprot.org/cit...rdfs:commentWe have determined the nucleotide sequences of the genes encoding the fimbrial subunits representative of the known Bacteroides nodosus serogroups. All of the genes are preceded by a highly conserved region which includes the likely promoter and transcriptional regulator sites as well as the ribosome-biding site, and are followed within a short but variable distance by a sequence with the characteristics of a transcription termination or attenuation signal. Based on sequence and organization, the subunits can be divided into two major classes called I (serogroups A, B, C, E, F, G, and I) and II (serogroups D and H). All contain the same seven-amino-acid positively charged leader sequence and conserved hydrophobic amino-terminal sequence typical of type 4 fibriae. Beyond this point the class II subunits are quite different from class I and share features more in common with those from other type 4 fimbriate bacteria, such as Moraxella bovis and Pseudomonas aeruginosa. The larger class I may be further subdivided into two subsets: (i) [A, E, F)(B, I)) and (ii) (C, G). These proteins exhibit three major clusters of variation, at either end of the presumptive disulphide loop which spans the central third of the protein, and near the carboxy-terimus, with dispersed changes in between. The length of the mature subunits varies from 152-156 amino acids, and the variation includes small insertions or deletions in the variable clusters between more conserved domains. The class II subunits are 149 amino acids in length and contain two pairs of cysteine residues: one is at the end of the amino-terminal conserved region, and the other is at the end of the protein. The major variation occurs in the central region of the molecule, and again small insertions or deletions are required to align adjacent conserved domains. There is also a striking absence of silent codon changes in the 5' coding region of all of these genes, indicating that these sequences have a secondary genetic function, probably in recombinational exchange.lld:uniprot
http://purl.uniprot.org/cit...skos:exactMatchhttp://purl.uniprot.org/med...lld:uniprot
http://purl.uniprot.org/cit...skos:exactMatchhttp://purl.uniprot.org/pub...lld:uniprot
http://purl.uniprot.org/cit...uniprot:nameMol. Microbiol.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorDalrymple B.P.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorMattick J.S.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorHobbs M.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorCox P.T.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorAnderson B.J.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorBills M.M.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorEgerton J.R.lld:uniprot
http://purl.uniprot.org/cit...uniprot:date1991lld:uniprot
http://purl.uniprot.org/cit...uniprot:pages561-573lld:uniprot
http://purl.uniprot.org/cit...uniprot:titleGene sequences and comparison of the fimbrial subunits representative of Bacteroides nodosus serotypes A to I: class I and class II strains.lld:uniprot
http://purl.uniprot.org/cit...uniprot:volume5lld:uniprot
http://purl.uniprot.org/cit...dc-term:identifierdoi:10.1111/j.1365-2958.1991.tb00727.xlld:uniprot
uniprot-protein:P17422uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P17823uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P17824uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P02975uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P17822uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P13253uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P17825uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P17826uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P11933uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P04953uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P17827uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
uniprot-protein:P27906uniprot:citationhttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot
http://linkedlifedata.com/r...rdf:objecthttp://purl.uniprot.org/cit...lld:uniprot