Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-10-26
pubmed:databankReference
pubmed:abstractText
A cosmid-based genomic library of Klebsiella pneumoniae 52145 (O1:K2) was introduced into Escherichia coli, and clones were screened for the bacteriocin 28b resistance phenotype. One clone was found which conferred partial resistance to bacteriocin 28b. By using Tn5tac1 insertions, it was shown that this phenotype was due to the expression, in E. coli, of an outer-membrane protein (OMP) with an apparent molecular mass of 17 kDa (OmpK17). The DNA region defined by insertion mutagenesis was sequenced and found to contain an ORF of 510 bp. The deduced amino acid sequence has 170 residues with a theoretical molecular mass of 18.4 kDa. The protein contains an N-terminal signal sequence of 24 amino acid residues. When compared with other enterobacterial OMPs, OmpK17 most closely resembles members of a family of small OMPs of Enterobacteriaceae the known functions of which appear to be related to virulence. Immunoblotting experiments showed that OmpK17 is also present in various K. pneumoniae strains belonging to different O and K serotypes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0923-2508
pubmed:author
pubmed:issnType
Print
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Molecular characterization of a 17-kDa outer-membrane protein from Klebsiella pneumoniae.
pubmed:affiliation
Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Barcelona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't