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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:P74901
Protein Name:VATE aka ATPE
Length:188
Molecular Weight:20616.00
Species:Thermus aquaticus (subsp [300852]
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate hydron

Cross database links:

RefSeq: YP_144542.1   
Entrez Gene ID: 3168454   
Pfam: PF01991   
BioCyc: TTHE300852:TTHA1276-MONOMER   
KEGG: ttj:TTHA1276   

Gene Ontology

GO:0033178 C:proton-transporting two-sector ATPase compl...
GO:0005524 F:ATP binding
GO:0046933 F:hydrogen ion transporting ATP synthase acti...
GO:0046961 F:proton-transporting ATPase activity, rotati...
GO:0042777 P:plasma membrane ATP synthesis coupled proto...

References (1)

[1] “V-type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon.”  Yokoyama K.et.al.   10788522
Structure:
3K5B   3J0J   3V6I   5gar   5GAS   5TSJ   5Y5X   5Y5Y   5Y5Z   5Y60   [...more]

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MSKLEAILSQ EVEAEIQALL QEAEAKAEAV KREAEEKAKA LLQARERALE AQYRAALRRA 
61:	ESAGELLVAT ARTQARGEVL EEVRRRVREA LEALPQKPEW PEVVRKLALE ALEALPGAKA 
121:	LVANPEDLPH LEALARERGV ELQAEPALRL GVRAVGAEGK TQVENSLLAR LDRAWDALSS 
181:	KVAQALWG