Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-6-9
pubmed:abstractText
An analysis of the distribution of the Na(+)-translocating ATPases/ATP synthases among microbial genomes identified an atypical form of the F(1)F(o)-type ATPase that is present in the archaea Methanosarcina barkeri and M. acetivorans, in a number of phylogenetically diverse marine and halotolerant bacteria and in pathogens Burkholderia spp. In complete genomes, representatives of this form (referred to here as N-ATPase) are always present as second copies, in addition to the typical proton-translocating ATP synthases. The N-ATPase is encoded by a highly conserved atpDCQRBEFAG operon and its subunits cluster separately from the equivalent subunits of the typical F-type ATPases. N-ATPase c subunits carry a full set of sodium-binding residues, indicating that most of these enzymes are Na(+)-translocating ATPases that likely confer on their hosts the ability to extrude Na(+) ions. Other distinctive properties of the N-ATPase operons include the absence of the delta subunit from its cytoplasmic sector and the presence of two additional membrane subunits, AtpQ (formerly gene 1) and AtpR (formerly gene X). We argue that N-ATPases are an early-diverging branch of membrane ATPases that, similarly to the eukaryotic V-type ATPases, do not synthesize ATP. Supplementary information: Supplementary data are available at Bioinformatics online.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-11152613, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-12225777, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-12835416, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-14740891, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-15173120, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-15802565, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-15860619, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-16522800, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-17351032, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-17442750, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-17912264, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-17938630, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-17986085, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18083842, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18252824, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18380897, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18417537, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18485887, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18573072, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18927115, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18940856, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-18984618, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-19303305, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-19500592, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-19796137, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-19892825, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-19920124, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-3112121, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-8169202, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-9254694, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-9425287, http://linkedlifedata.com/resource/pubmed/commentcorrection/20472544-9608053
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1367-4811
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1473-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase.
pubmed:affiliation
School of Physics, University of Osnabrück, D-49069 Osnabrück, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Intramural