| Type | Description |
|---|---|
| Definition | ATP synthase Fo complex subunit b |
| Date | Results | Publications |
|---|---|---|
| 2019-08-10 10:18:00 | Mutation betaL249Q significantly enhanced ADP-inhibition in E. coli ATP synthase, increased the extent of ATP hydrolysis stimulation by sulfite, and rendered the ADP-inhibition sensitive to phosphate in the same manner as observed in FOF1 from mitochondria, chloroplasts, and most aerobic\photosynthetic bacteria. | 30528692 |
| 2013-05-25 12:06:00 | Data indicate the juxtaposition of subunits b and a in the ATP synthase. | 23416299 |
| 2010-01-21 00:00:00 | subunit b dimer of the FOF1-ATP synthase interacts with F1-ATPase | 15339903 |
| 2010-01-21 00:00:00 | The first solution structure of b30-82, including the tether region and part of the dimerization domain, has been solved by nuclear magnetic resonance, revealing an alpha-helix between residues 39 and 72. | 19820091 |
| 2010-01-21 00:00:00 | The results indicate a right-handed coiled-coil structure with intrinsic asymmetry, the two helices being offset rather than in register. A function for the right-handed coiled coil in rotational catalysis is proposed. | 17028022 |
| Type | IDs |
|---|---|
| Synonymous | ECK3729, papF, uncF |
| Gene |
UniProtKB-ID:
ATPF_ECOLI
UniprotKB:
P0ABA0
UniParc:
UPI000003EAF6
EMBL:
V00266,
M25464,
X01631,
L10328,
V00310,
J01594,
M12212,
AP009048,
M10422,
V00264,
U00096
EnsemblGenome:
b3736,
BAE77552
KO:
ecj:JW3714,
eco:b3736
|
| Nucleutide sequences |
EMBL-CDS:
BAE77552.1,
AAA24741.1,
AAA24733.1,
CAA23516.1,
AAA62088.1,
CAA23523.1,
CAA23592.1,
CAA25778.1,
AAA83871.1,
AAA20043.1,
AAC76759.1
EnsemblGenome_TRS:
AAC76759,
BAE77552
|
| Protein sequencees |
EnsemblGenome_PRO:
BAE77552,
AAC76759
RefSeq:
NP_418192.1
|
| Others |
UniRef100:
UniRef100_A7ZTU8
UniRef90:
UniRef90_Q6CYJ1
UniRef50:
UniRef50_Q6CYJ1
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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