⊟Summary[edit | edit source]
- pan ID?: SAUPAN005397000
- symbol?: atpH
- synonym:
- description?: F0F1 ATP synthase subunit delta
- F0F1 ATP synthase subunit delta
- ATP synthase subunit delta
- ATP synthase F0F1 subunit delta
- FOF1-ATP synthase, subunit delta
- ATP synthase delta chain
- ATP synthase F1, delta subunit
- ATP synthase F1 sector delta subunit
- ATP synthase F1 subunit delta
- putative ATP synthase delta chain
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5559905..5560444
- synteny block?: BlockID0041930
- occurrence?: in 100% of 34 strains
atpH : F0F1 ATP synthase subunit delta [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. AtpH encodes F1 subunit δ, the "solder" protein linking F0 and F1 complexes through binding the F0 subunit B "brace" protein and the F1 α3β3 hexamer. This maintains a functional association counteracting the free-rotation torque applied by the central stalk rotor.
⊟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 MVKVANKYAKALFDVSLDTNNLETINEELTVINEAVKDKIEQLRMVDSNPTQTAEQRREL
N315 MVKVANKYAKALFDVSLDTNNLETINEELTVINEAVKDKIEQLKMVDSNPTQTAEQRREL
NCTC8325 MVKVANKYAKALFDVSLDTNNLETINEELTVINEAVKDKIEQLRMVDSNPTQTAEQRREL
Newman MVKVANKYAKALFDVSLDTNNLETINEELTVINEAVKDKIEQLRMVDSNPTQTAEQRREL
USA300_FPR3757 MVKVANKYAKALFDVSLDTNNLETINEELTVINEAVKDKIEQLRMVDSNPTQTAEQRREL
*******************************************:****************
COL INGVFTDINPYIKNMMYVLADNRHISLIADVFKAFQSLYNGHYNQDFATIESTYELSQEE
N315 INGVFTDINPYIKNMMYVLADNRHISLIADVFKAFQSLYNGHYNQDFATIESTYELSQEE
NCTC8325 INGVFTDINPYIKNMMYVLADNRHISLIADVFKAFQSLYNGHYNQDFATIESTYELSQEE
Newman INGVFTDINPYIKNMMYVLADNRHISLIADVFKAFQSLYNGHYNQDFATIESTYELSQEE
USA300_FPR3757 INGVFTDINPYIKNMMYVLADNRHISLIADVFKAFQSLYNGHYNQDFATIESTYELSQEE
************************************************************
COL LDKIVKLVTQQTKLSKVIVDTKINPDLIGGFRVKVGTTVLDGSVRNDLVQLQRKFRRVN
N315 LDKIVKLVTQQTKLSKVIVDTKINPDLIGGFRVKVGTTVLDGSVRNDLVQLQRKFRRVN
NCTC8325 LDKIVKLVTQQTKLSKVIVDTKINPDLIGGFRVKVGTTVLDGSVRNDLVQLQRKFRRVN
Newman LDKIVKLVTQQTKLSKVIVDTKINPDLIGGFRVKVGTTVLDGSVRNDLVQLQRKFRRVN
USA300_FPR3757 LDKIVKLVTQQTKLSKVIVDTKINPDLIGGFRVKVGTTVLDGSVRNDLVQLQRKFRRVN
***********************************************************
- ↑ 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)