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292  structures 5907  species 1  interaction 10204  sequences 24  architectures

Family: ATP-synt_C (PF00137)

Summary: ATP synthase subunit C

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This is the Wikipedia entry entitled "ATP synthase subunit C". More...

ATP synthase subunit C Edit Wikipedia article

2bl2.gif
V-type sodium ATPase from Enterococcus hirae. Calculated hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots
Identifiers
Symbol ATP-synt_C
Pfam PF00137
InterPro IPR002379
PROSITE PDOC00526
SCOP 1aty
SUPERFAMILY 1aty
OPM superfamily 5
OPM protein 2bl2

ATPase, subunit C of F0/V0 complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases.

ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport.[1][2]

  • F-ATPases (F1F0-ATPases) in mitochondria, chloroplasts and bacterial plasma membranes are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPase (V1V0-ATPases) are primarily found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport solutes and lower pH in organelles.
  • A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.
  • P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

The F-ATPases (or F1F0-ATPases) and V-ATPases (or V1V0-ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0 or V0 complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis.[3][4]

Subunit C (also called subunit 9, or proteolipid in F-ATPases, or the 16 kDa proteolipid in V-ATPases) was found in the F0 or V0 complex of F- and V-ATPases, respectively. In F-ATPases, ten C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the C subunit 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 subunit ring of F0. The sequential protonation and deprotonation of Asp61 of subunit C is coupled to the stepwise movement of the rotor.[5]

In V-ATPases, there are three proteolipid subunits (c, c and c) that form part of the proton-conducting pore, each containing a buried glutamic acid residue that is essential for proton transport, and together they form a hexameric ring spanning the membrane.[6][7]

In a recent study c-subunit has been indicated as a critical component of the mitochondrial permeability transition pore. [8]

Subfamilies[edit]

Human proteins containing this domain[edit]

ATP5G1; ATP5G2; ATP5G3; ATP6V0B; ATP6V0C;

References[edit]

  1. ^ Muller V, Cross RL (2004). "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio". FEBS Lett. 576 (1): 1–4. doi:10.1016/j.febslet.2004.08.065. PMID 15473999. 
  2. ^ Zhang X, Niwa H, Rappas M (2004). "Mechanisms of ATPases--a multi-disciplinary approach". Curr Protein Pept Sci 5 (2): 89–105. doi:10.2174/1389203043486874. PMID 15078220. 
  3. ^ Itoh H, Yoshida M, Yasuda R, Noji H, Kinosita K (2001). "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase". Nature 410 (6831): 898–904. doi:10.1038/35073513. PMID 11309608. 
  4. ^ Wilkens S, Zheng Y, Zhang Z (2005). "A structural model of the vacuolar ATPase from transmission electron microscopy". Micron 36 (2): 109–126. doi:10.1016/j.micron.2004.10.002. PMID 15629643. 
  5. ^ Fillingame RH, Angevine CM, Dmitriev OY (2003). "Mechanics of coupling proton movements to c-ring rotation in ATP synthase". FEBS Lett. 555 (1): 29–34. doi:10.1016/S0014-5793(03)01101-3. PMID 14630314. 
  6. ^ Inoue T, Forgac M (2005). "Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain". J. Biol. Chem. 280 (30): 27896–27903. doi:10.1074/jbc.M504890200. PMID 15951435. 
  7. ^ Jones R, Findlay JB, Harrison M, Durose L, Song CF, Barratt E, Trinick J (2003). "Structure and function of the vacuolar H+-ATPase: moving from low-resolution models to high-resolution structures". J. Bioenerg. Biomembr. 35 (4): 337–345. doi:10.1023/A:1025728915565. PMID 14635779. 
  8. ^ Bonora, M; Bononi, A; De Marchi, E; Giorgi, C; Lebiedzinska, M; Marchi, S; Patergnani, S; Rimessi, A; Suski, JM; Wojtala, A; Wieckowski, MR; Kroemer, G; Galluzzi, L; Pinton, P (2013 Feb 15). "Role of the c subunit of the FO ATP synthase in mitochondrial permeability transition.". Cell cycle (Georgetown, Tex.) 12 (4): 674–83. PMID 23343770. 

This article incorporates text from the public domain Pfam and InterPro [1]

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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ATP synthase subunit C Provide feedback

No Pfam abstract.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002379

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [PUBMED:15473999, PUBMED:15078220]. The different types include:

  • F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases (though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases).
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

The F-ATPases (or F1F0-ATPases) and V-ATPases (or V1V0-ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0 or V0 complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [PUBMED:11309608, PUBMED:15629643].

This entry represents subunit C (also called subunit 9, or proteolipid in F-ATPases, or the 16 kDa proteolipid in V-ATPases) found in the F0 or V0 complex of F- and V-ATPases, respectively. In F-ATPases, ten C subunits form an oligomeric ring that makes up the F0 rotor. The flux of protons through the ATPase channel drives the rotation of the C subunit 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 subunit ring of F0. The sequential protonation and deprotonation of Asp61 of subunit C is coupled to the stepwise movement of the rotor [PUBMED:14630314].

In V-ATPases, there are three proteolipid subunits (c, c' and c'') that form part of the proton-conducting pore, each containing a buried glutamic acid residue that is essential for proton transport, and together they form a hexameric ring spanning the membrane [PUBMED:15951435, PUBMED:14635779].

Structurally, the c subunits consist of a two antiparallel transmembrane helices. Both helices of one c subunit are connected by a loop on the cytoplasmic side [PUBMED:19783985].

More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].

Gene Ontology

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Domain organisation

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Alignments

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  Seed
(167)
Full
(10204)
Representative proteomes NCBI
(5928)
Meta
(2123)
RP15
(1106)
RP35
(1902)
RP55
(2580)
RP75
(3091)
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  Seed
(167)
Full
(10204)
Representative proteomes NCBI
(5928)
Meta
(2123)
RP15
(1106)
RP35
(1902)
RP55
(2580)
RP75
(3091)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Curation and family details

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Seed source: Prosite
Previous IDs: none
Type: Family
Author: Sonnhammer ELL
Number in seed: 167
Number in full: 10204
Average length of the domain: 66.90 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 77.67 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.3 21.3
Noise cut-off 21.2 21.2
Model length: 66
Family (HMM) version: 16
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Species distribution

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Interactions

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ATP-synt_C

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ATP-synt_C domain has been found. There are 292 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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