Type | Description |
---|---|
Definition | ATP synthase F1 complex subunit beta |
Date | Results | Publications |
---|---|---|
2012-09-15 10:23:00 | The results show that beta/gamma rotor-stator interactions near the gamma carboxyl terminus and at the gammaMet23-betaDELSEED both contribute to formation of the rate-limiting transition state of rotational catalysis. | 22582396 |
2012-04-07 10:27:00 | the interaction of F(0)F(1) ATP synthase with FliG is important for the function of the switch of bacterial flagella | 22210351 |
2010-06-28 11:58:00 | Homology modeling indicates that the amino acid replacement induces a hydrophobic network, in which the betaMet159, betaIle163, and betaAla167 residues of the beta subunit are involved together with the mutant betaPhe174. | 20331967 |
2010-01-21 00:00:00 | These results imply that the polypeptide in the b N-terminus position is more important for F1 binding than the one in the b C-terminus position and illustrate the significance of the asymmetry of the b dimer in the enzyme. | 17766239 |
2010-01-21 00:00:00 | The authors identified a knockout of atpD, coding for a component of the F(o)F(1) ATPase, as defective in Ca(2+) efflux. | 19481094 |
Type | IDs |
---|---|
Synonymous | ECK3725, papB, uncD |
Gene |
UniProtKB-ID:
ATPB_ECOLI
UniprotKB:
P0ABB4
UniParc:
UPI000003EAF2
EMBL:
AP009048,
V00312,
U00096,
V00311,
V00267,
M25464,
J01594,
L10328,
X01631
EnsemblGenome:
b3732,
BAE77556
KO:
eco:b3732,
ecj:JW3710
|
Nucleutide sequences |
EMBL-CDS:
CAA23527.1,
CAA23594.1,
AAC76755.1,
CAA25782.1,
AAA24737.1,
CAA23598.1,
AAA62084.1,
BAE77556.1,
AAA83875.1
EnsemblGenome_TRS:
AAC76755,
BAE77556
|
Protein sequencees |
EnsemblGenome_PRO:
AAC76755,
BAE77556
RefSeq:
NP_418188.1
|
Others |
UniRef100:
UniRef100_A7ZTU4
UniRef90:
UniRef90_Q6CYJ5
UniRef50:
UniRef50_Q8E8C0
|
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---|---|---|---|---|---|---|---|---|
Refseq |
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