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3.A.2.2.1
H+-translocating V-type ATPase. The 3-D structure is known (Lau and Rubinstein, 2012). More recently, Zhou and Sazanov 2019 solved cryo-EM structures of the intact Thermus thermophilus V/A-ATPase in three rotational states with two substates. These structures indicate substantial flexibility between V1 and Vo in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks.

Accession Number:P74900
Protein Name:VATL-THERM
Length:99
Molecular Weight:9836.00
Species:Thermus thermophilus [274]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate hydron

Cross database links:

Pfam: PF00137   

Gene Ontology

GO:0033179 C:proton-transporting V-type ATPase, V0 domain
GO:0015078 F:hydrogen ion transmembrane transporter acti...
GO:0015986 P:ATP synthesis coupled proton transport

References (1)

[1] “V-type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon.”  Yokoyama K.et.al.   10788522

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MKKLLVTVLL AVFGALAFAA EEAAASGGLD RGLIAVGMGL AVGLAALGTG VAQARIGAAG 
61:	VGAIAEDRSN FGTALIFLLL PETLVIFGLL IAFILNGRL