V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 661567364  49 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 111
Cdd:cd18177    1 WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63

V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 661567364  49 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 111
Cdd:cd18177    1 WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63

ATP synthase subunit C;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 661567364  138 FGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 196
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59

V-type ATP synthase subunit K; Validated

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661567364  45 SPFMWSNLGIGLAISLSVVgAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIsnMAEPFSATDPK 124
Cdd:PRK06271  68 TAPEWAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAILL--LVGVFASPGVE 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661567364 125 AIGhrnyhagysMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 196
Cdd:PRK06271 145 TIA---------ALGAGLAVGFAGL-SGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFAIFGLLIAIL 206

FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K is part of the Pathway/BioSystem: FoF1-type ATP synthase

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 661567364 133 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSA----IGLFGVIVAIL 196
Cdd:COG0636    3 AAASAIGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAAlieaLAIYALVIALI 70

V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 661567364  49 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 111
Cdd:cd18177    1 WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63

V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 661567364 133 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 196
Cdd:cd18176    3 KGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALI 66

ATP synthase subunit C;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 661567364   52 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 111
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60

Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase subunit c. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and functions like the F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. The V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. The V1 complex consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The Vo complex consists of five different subunits: a, c, c', c'', and d. The Ao/A1 complexes are composed of nine subunits in a stoichiometry of A(3):B(3):C:D:E:F:H(2):a:c(x). ATP is synthesized on the A3:B3 hexamer and the energy released during that process is transferred to the Ao complex, which consists of the C-terminal segment of subunit a and subunit c.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661567364  51 NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 111
Cdd:cd18120    2 YLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62

V-type ATP synthase subunit K; Validated

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661567364  45 SPFMWSNLGIGLAISLSVVgAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIsnMAEPFSATDPK 124
Cdd:PRK06271  68 TAPEWAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAILL--LVGVFASPGVE 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661567364 125 AIGhrnyhagysMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 196
Cdd:PRK06271 145 TIA---------ALGAGLAVGFAGL-SGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFAIFGLLIAIL 206

ATP synthase, membrane-bound Fo/Vo/Ao complexes, subunit c; Subunit c of the Fo/Vo/Ao complex is the main transmembrane subunit of F-, V- or A-type family of ATP synthases with rotary motors. These ion-transporting rotary ATP synthases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contains three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao (oligomycin sensitive) complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and function like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 661567364 137 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPS----LFVKILIVEIFGSAIGLFGVIVAIL 196
Cdd:cd00313    1 ALGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPEaagkIFTTMLIGLALIESLAIYGLVIAFL 64

V-type ATP synthase subunit K; Validated

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661567364  48 MWSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGII----MAIVISNMAEPFSATDP 123
Cdd:PRK08344   1 VYVALGAALAAGLAGAASSFGVGIAGSAAAGAVAEDEKNFRNALILAGLPMTQTIYGLItlflILMYAGILGGGFKFAEP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 661567364 124 KAIghrNYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNP-SLFVKILIVEIFGSAIGLFGVIVAILQVM 199
Cdd:PRK08344  81 DTI---NLGKALALLGAGLLVGLAELLSAIPQGIICASGIGALPRTPgKTFTQTIILAAYAELMGIFGLVFAILGLS 154

membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or proteolipid) of the Fo complex of F-ATP synthase. The F-ATP synthase (also called FoF1-ATPase) consists of two structural domains: the F1 (factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons though the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Methanosarcina acetivorans.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 661567364  52 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAP----RIKTKNLVSIIFCEAVAIYGIIMAIVI 111
Cdd:cd18121    2 LGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPeaagKIRTTMIIGLALIESLAIYALVIALIL 65

V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661567364  51 NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIS 112
Cdd:cd18176    7 HLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS 68

membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or proteolipid) of the Fo complex of F-ATP synthase. The F-ATP synthase (also called FoF1-ATPase) consists of two structural domains: the F1 (factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons though the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Methanosarcina acetivorans.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 661567364 137 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSA----IGLFGVIVAIL 196
Cdd:cd18121    1 ALGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLAliesLAIYALVIALI 64

V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+)-translocating ATPase subunit K, or sodium ATPase proteolipid component) is involved in ATP-driven sodium extrusion.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 661567364 134 GYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 196
Cdd:cd18180    1 GLAILGAGLPVGIVGLFSAIYQGKVAAAGIGAVAKRPEEFGKAIILAAMVETYAILGLLISIL 63