Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase.
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.


BACKGROUND
Supplementary data are available at Bioinformatics online.
Dibrova
Daria V
DV
School of Physics, University of Osnabrück, D-49069 Osnabrück, Germany.
Galperin
Michael Y
MY
Mulkidjanian
Armen Y
AY
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D027682:Cation Transport Proteins / Q000737:chemistry*; D016680:Genome, Bacterial
D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D000251:Adenosine Triphosphatases; C021838:sodium-translocating ATPase
J Mol Biol. 2009 Aug 14;391(2):498-507
19500592
Nucleic Acids Res. 2010 Jan;38(Database issue):D211-22
19920124
Nat Rev Microbiol. 2007 Nov;5(11):892-9
17938630
Nucleic Acids Res. 2009 Jan;37(Database issue):D32-6
18927115
J Bacteriol. 2007 May;189(10):3759-67
17351032
J Mol Evol. 1998 Jun;46(6):703-15
9608053
Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):985-92
18485887
Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):2005-10
18252824
Nucleic Acids Res. 1997 Sep 1;25(17):3389-402
9254694
Brief Bioinform. 2008 Jul;9(4):299-306
18417537
Science. 2005 Apr 29;308(5722):654-9
15802565
Nat Rev Mol Cell Biol. 2007 Nov;8(11):917-29
17912264
Proc Natl Acad Sci U S A. 2007 May 1;104(18):7600-5
17442750
Biochem Biophys Res Commun. 1997 Dec 18;241(2):427-33
9425287
Proc Natl Acad Sci U S A. 2007 Dec 26;104(52):20776-81
18083842
Annu Rev Biophys. 2008;37:43-64
18573072
Nucleic Acids Res. 2009 Jan;37(Database issue):D211-5
18940856
Trends Biochem Sci. 2009 Apr;34(4):206-15
19303305
Nucleic Acids Res. 2009 Jan;37(Database issue):D205-10
18984618
Nucleic Acids Res. 2010 Jan;38(Database issue):D340-5
19892825
Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8298-303
12835416
J Bacteriol. 1987 Aug;169(8):3429-34
3112121
Genome Res. 2004 Jun;14(6):1188-90
15173120
J Bioenerg Biomembr. 2003 Oct;35(5):427-37
14740891
FEMS Microbiol Lett. 2009 Nov;300(2):230-6
19796137
Biol Direct. 2008 Apr 01;3:13
18380897
Science. 2005 Apr 29;308(5722):659-62
15860619
J Mol Biol. 2001 Jan 19;305(3):567-80
11152613
J Bacteriol. 1994 May;176(9):2543-50
8169202
Protein Sci. 2006 Apr;15(4):935-41
16522800
FEMS Microbiol Lett. 2007 Dec;277(1):56-63
17986085
Prog Biophys Mol Biol. 2002 May-Jul;79(1-3):77-133
12225777