| Protein name |
ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) |
| NCBI Accession ID |
BX908798.1 |
| Organism |
Protochlamydia amoebophila (strain UWE25) |
| Left |
2010953 |
| Right |
2011249 |
| Strand |
- |
| Nucleotide Sequence |
ATGCATTTAGCACGAAATCCAGCCCTGAAAAGCATTTACATTAAAATAAGAAAGAGGAAAACAATGAGTATTGGAACAGCATTAGCTCTCTCTGCTCCATTTGCAGTCGGTCTTGCAGCATTAGGATCAGGTCTTGGTCTTGGTCGTGCTGTGAGTAGTGCAATGGAAGCTATAGGTCGTCAACCTGAAGCATCTGGTAAAATTTTGACGACAATGATTATTGGCGCTGCTTTGATTGAAGCCCTAACAATTTATGCTTTAATTGTGTTCTTCGTTGTTTTAGAAAAAATGGCATAA |
| Sequence |
MHLARNPALKSIYIKIRKRKTMSIGTALALSAPFAVGLAALGSGLGLGRAVSSAMEAIGRQPEASGKILTTMIIGAALIEALTIYALIVFFVVLEKMA |
| Source of smORF |
Swiss-Prot |
| Function |
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-Rule:MF_01396}.; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. {ECO:0000255|HAMAP-Rule:MF_01396}. |
| Pubmed ID |
15073324
|
| Domain |
CDD:412393 |
| Functional Category |
Others |
| Uniprot ID |
Q6MAK2
|
| ORF Length (Amino Acid) |
98 |