Immunotation of Rv1304
From DrugPedia: A Wikipedia for Drug discovery
| Immunotation of Rv1304
| |
| Name | |
| F0F1 ATP synthase subunit A | |
| Identifiers | |
| Swiss Prot | |
| Genbank | |
| PDB | ? |
| Chemical data | |
| Formula | ? |
| Mol. wt. | 27466.3Da |
| Pharmacokinetic data | |
| Bioavailability | ? |
| Solubility | ? |
| Isoelectric-Point | 6.6 |
Contents |
General
F0F1-ATP synthase couples ATP synthesis/hydrolysis with transmembrane proton transport. The catalytic mechanism involves rotation of the γεc∼10-subunits complex relative to the rest of the enzyme. In the absence of protonmotive force the enzyme is inactivated by the tight binding of MgADP. Subunit ε also modulates the activity: its conformation can change from a contracted to extended form with C-terminus stretched towards F1. The latter form ihnibits ATP hydrolysis (but not synthesis). Block of rotation by MgADP presumably induces the extended conformation of subunit ε. This conformation might serve as a safety lock, stabilizing the ADP-inhibited state upon de-energization and preventing spontaneous re-activation and wasteful ATP hydrolysis. The hypothesis merges the known regulatory effects of ADP, protonmotive force and conformational changes of subunit ε into a consistent picture. The transmembrane electrochemical proton gradient generated by the redox systems of the respiratory chain in mitochondria and aerobic bacteria is utilized by proton translocating ATP synthases to catalyze the synthesis of ATP from ADP and P(i). The bacterial and mitochondrial H(+)-ATP synthases both consist of a membranous sector, F0, which forms a H(+)-channel, and an extramembranous sector, F1, which is responsible for catalysis. When detached from the membrane, the purified F1 sector functions mainly as an ATPase. In chloroplasts, the synthesis of ATP is also driven by a proton motive force, and the enzyme complex responsible for this synthesis is similar to the mitochondrial and bacterial ATP synthases. The synthesis of ATP by H(+)-ATP synthases proceeds without the formation of a phosphorylated enzyme intermediate, and involves co-operative interactions between the catalytic subunits.
Protein Sequence
>Rv1304, TB.seq 1460242:1460991 MW:27467 MTETILAAQIEVGEHHTATWLGMTVNTDTVLSTAIAGLIVIALAFYLRAKVTSTDVPGGVQLFFEAITIQMRNQVESAIG MRIAPFVLPLAVTIFVFILISNWLAVLPVQYTDKHGHTTELLKSAAADINYVLALALFVFVCYHTAGIWRRGIVGHPIKL LKGHVTLLAPINLVEEVAKPISLSLRLFGNIFAGGILVALIALFPPYIMWAPNAIWKAFDLFVGAIQAFIFALLTILYFS QAMELEEEHH
Human Homologue Blast Result
| subject ids | % identity | % positives | alignment length | evalue |
| sp|Q08945 | 60 | 69 | 23 | 1.7 |
| sp|P00846 | 26 | 46 | 162 | 2.0 |
| sp|Q8WYA6 | 27 | 41 | 74 | 2.8 |
| sp|Q6P2P2 | 35 | 54 | 51 | 8.6 |
Alergen Protein
Link to Algpred
Non Allergen Predicted by AlgPred Server
Bacterial Toxin Prediction
Link to btxpred
No Hit Found by btxpred server.
Subcellular Location
Link to TBpred
INTEGRAL MEMBRANE PROTEIN
Antigens
No Hit Found in AntigenDB
No. Hit Found in IEDB
B cell Epitopes
BCEpred Analysis
Link to Bcepred
Result Predicited by [1]
ABCpred Analysis
Link to ABCpred
Result Predicited by [2]
IEDB Analysis
Link to IEDB
Result Predicited by [3]
MHC Class-I Binder
nHLAPred Analysis
Link to nHLApred
Result Predicited by [4]
IEDB Analysis
Link to IEDB
Result Predicted by [5]
MHC Class-II Binder
Propred Analysis
Link to Propred
Result Predicted by []
NetMHC-II Analysis
Link to NetMHC-II
Result Predicted by []
External Links
- Database of Mycobacterium tuberculosis genome sequences and related information.
