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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:P74902
Protein Name:VATC aka ATPC
Length:323
Molecular Weight:35919.00
Species:Thermus aquaticus (subsp [300852]
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate hydron

Cross database links:

RefSeq: YP_144541.1   
Entrez Gene ID: 3168086   
Pfam: PF01992   
BioCyc: TTHE300852:TTHA1275-MONOMER   
KEGG: ttj:TTHA1275   

Gene Ontology

GO:0033177 C:proton-transporting two-sector ATPase compl...
GO:0005524 F:ATP binding
GO:0046933 F:hydrogen ion transporting ATP synthase acti...
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:
1R5Z   1V9M   3J0J   5GAR   5GAS   5TSJ   5Y5X   5Y5Y   5Y5Z   5Y60   [...more]

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence 
1:	MADDFAYLNA RVRVRRGTLL KESFFQEALD LSFADFLRLL SETVYGGELA GQGLPDVDRA 
61:	VLRTQAKLVG DLPRLVTGEA REAVRLLLLR NDLHNLQALL RAKATGRPFE EVLLLPGTLR 
121:	EEVWRQAYEA QDPAGMAQVL AVPGHPLARA LRAVLRETQD LARVEALLAK RFFEDVAKAA 
181:	KGLDQPALRD YLALEVDAEN LRTAFKLQGS GLAPDAFFLK GGRFVDRVRF ARLMEGDYAV 
241:	LDELSGTPFS GLSGVRDLKA LERGLRCVLL KEAKKGVQDP LGVGLVLAYV KEREWEAVRL 
301:	RLLARRAYFG LPRAQVEEEV VCP