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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:P74899
Protein Name:VATI-THERM
Length:648
Molecular Weight:71733.00
Species:Thermus thermophilus [274]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate H+

Cross database links:

Pfam: PF01496   

Gene Ontology

GO:0033177 C:proton-transporting two-sector ATPase compl...
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

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MEKLVLAGPK GRAKELLQSL QQAGVVHLET LRPEALSAYQ LSPEERAELR RWEAVSAGAE 
61:	HTLSLLGLEA EPARPFPEGL EAAEKALSPI QAHAEGLTRQ KQELEEELAL AQAYLEPLER 
121:	LAALAHGLDK SPFLRVIPFL LTEKELPLVE EALRKALEDR YLLAHEAYAG GVPALVVVHR 
181:	KEVDQAKAAL SRAGVAELRL PGALGELPLS EAARRLKERA EAAPRELSEV RQHLAKLARE 
241:	SASTLQSLWT RAQDEVARLK ALEELASGRF GFALLGYVPV KAKPKVEEAL ARHKESVVYA 
301:	FEPVDEHHEA DRIPVVLDNP PWAKPFELLV SFLNTPKYGT FDPTPVVPVF FPFWFGMIVG 
361:	DIGYALLFYL VGRWLSGYVK RNEPLVIDLF ALKLKPQVIG KLVHILNWMV FWTVVWGVIY 
421:	GEFFGTFLEH LGVFGTPEHP GLIPILIHRI DTAKTANLLI LLSVAFGVVL VFFGLALRAY 
481:	LGLKHRHMAH FWEGVGYLGG LVGVLALAAS YLGNLQAGWL QGLMYLGFGV FLLAVLMSRI 
541:	WLMIPEIFTQ AGHILSHIRI YAVGAAGGIL AGLLTDVGFA LAERLGLLGV LLGLLVAGVL 
601:	HLLILLLTTL GHMLQPIRLL WVEFFTKFGF YEENGRPYRP FKSVREAQ