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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:Q56404
Protein Name:V-type ATP synthase beta chain
Length:478
Molecular Weight:53160.00
Species:Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [300852]
Substrate H+

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  • 2° Structure (Network Protein Sequence Analysis)

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FASTA formatted sequence
1:	MDLLKKEYTG ITYISGPLLF VENAKDLAYG AIVDIKDGTG RVRGGQVIEV SEEYAVIQVF 
61:	EETTGLDLAT TSVSLVEDVA RLGVSKEMLG RRFNGIGKPI DGLPPITPEK RLPITGLPLN 
121:	PVARRKPEQF IQTGISTIDV MNTLVRGQKL PIFSGSGLPA NEIAAQIARQ ATVRPDLSGE 
181:	GEKEEPFAVV FAAMGITQRE LSYFIQEFER TGALSRSVLF LNKADDPTIE RILTPRMALT 
241:	VAEYLAFEHD YHVLVILTDM TNYCEALREI GAAREEIPGR RGYPGYMYTD LATIYERAGV 
301:	VEGKKGSVTQ IPILSMPDDD RTHPIPDLTG YITEGQIQLS RELHRKGIYP PIDPLPSLSR 
361:	LMNNGVGKGK TREDHKQVSD QLYSAYANGV DIRKLVAIIG EDALTENDRR YLQFADAFER 
421:	FFINQGQQNR SIEESLQIAW ALLSMLPQGE LKRISKDHIG KYYGQKLEEI WGAPQALD