⊟Summary[edit | edit source]
- pan ID?: SAUPAN005393000
- symbol?: atpC
- synonym:
- description?: F0F1 ATP synthase subunit epsilon
- F0F1 ATP synthase subunit epsilon
- ATP synthase epsilon chain
- ATP synthase F0F1 subunit epsilon
- FOF1-ATP synthase, subunit epsilon
- ATP synthase epsilon chain, AtpE
- ATP synthase F1, epsilon subunit
- ATP synthase F1 sector epsilon subunit
- ATP synthase F1 subunit epsilon
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5555620..5556024
- synteny block?: BlockID0041890
- occurrence?: in 100% of 34 strains
atpC : F0F1 ATP synthase subunit epsilon [1]
ATP synthases couple proton translocation across membranes to rotational energy, conformational change and, ultimately, ATP generation. The F0 portion is a multimeric membrane-embedded proton channel (ab2c10) while the F1 portion is a multimeric cytoplasmic structure (α3β3γδε) that binds ADP and phosphate. When necessary, this process can also be run in reverse to generate a proton gradient at the expense of ATP. AtpC encodes F1 subunit ε, the regulatory-moderator component of the overall macromolecular complex. This allows the cell to calibrate the F0F1 ATPase efficiency to match the needs of the cell. The ATP-bound ε subunit "spanner" physically blocks rotation of the central stalk rotor when intracellular ATP availability is high.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MNTLNLDIVTPNGSVYNRDNVELVVMQTTAGEIGVMSGHIPTVAALKTGFVKVKFHDGTE
N315 MNTLNLDIVTPNGSVYNRDNVELVVMQTTAGEIGVMSGHIPTVAALKTGFVKVKFHDGTE
NCTC8325 MNTLNLDIVTPNGSVYNRDNVELVVMQTTAGEIGVMSGHIPTVAALKTGFVKVKFHDGTE
Newman MNTLNLDIVTPNGSVYNRDNVELVVMQTTAGEIGVMSGHIPTVAALKTGFVKVKFHDGTE
USA300_FPR3757 MNTLNLDIVTPNGSVYNRDNVELVVMQTTAGEIGVMSGHIPTVAALKTGFVKVKFHDGTE
************************************************************
COL YIAVSDGFVEVRKDKVSIIVQTAETAREIDVERAKLAKARAESHLENDDDNTDIHRAERA
N315 YIAVSDGFVEVRKDKVSIIVQTAETAREIDVERAKLAKARAESHLENDDDNTDIHRAERA
NCTC8325 YIAVSDGFVEVRKDKVSIIVQTAETAREIDVERAKLAKARAESHLENDDDNTDIHRAERA
Newman YIAVSDGFVEVRKDKVSIIVQTAETAREIDVERAKLAKARAESHLENDDDNTDIHRAERA
USA300_FPR3757 YIAVSDGFVEVRKDKVSIIVQTAETAREIDVERAKLAKARAESHLENDDDNTDIHRAERA
************************************************************
COL LERANNRLRVAELK
N315 LERANNRLRVAELK
NCTC8325 LERANNRLRVAELK
Newman LERANNRLRVAELK
USA300_FPR3757 LERANNRLRVAELK
**************
- ↑ G Deckers-Hebestreit, K Altendorf
The F0F1-type ATP synthases of bacteria: structure and function of the F0 complex.
Annu Rev Microbiol: 1996, 50;791-824
[PubMed:8905099] [WorldCat.org] [DOI] (P p)Martin Vestergaard, Sahar Roshanak, Hanne Ingmer
Targeting the ATP Synthase in Staphylococcus aureus Small Colony Variants, Streptococcus pyogenes and Pathogenic Fungi.
Antibiotics (Basel): 2021, 10(4);
[PubMed:33918382] [WorldCat.org] [DOI] (P e)