| Type | Description |
|---|---|
| Definition | flagellar motor stator protein MotA |
| Date | Results | Publications |
|---|---|---|
| 2019-10-19 12:33:00 | These results suggest that MotA-Met206 is responsible for not only load-dependent energy coupling between the proton influx and rotation but also pH-dependent stator assembly. | 30642987 |
| 2014-11-22 10:56:00 | results suggest that the MotA/B complex is a load-sensitive proton channel that efficiently couples proton translocation with the conformational changes that generate torque | 24255940 |
| 2010-05-03 11:41:00 | The proton-conductivity of a Salmonella MotA/B complex not incorporated into the motor is two orders of magnitude lower than that of a complex that is incorporated and activated. | 20178785 |
| 2010-01-21 00:00:00 | Data propose that Pro173 residue of MotA plays an important role in facilitating the conformational dynamics of the stator complex for rapid proton translocation and torque generation cycle. | 19683537 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
MOTA_SALTY
UniprotKB:
P55891
UniParc:
UPI000012F3D5
EMBL:
U81861,
AE006468,
D43640
EnsemblGenome:
STM1923
KO:
stm:STM1923
|
| Nucleutide sequences |
EMBL-CDS:
AAL20839.1,
BAA85316.1,
AAC45265.1
EnsemblGenome_TRS:
AAL20839
|
| Protein sequencees |
EnsemblGenome_PRO:
AAL20839
RefSeq:
NP_460880.1
|
| Others |
UniRef100:
UniRef100_P55891
UniRef90:
UniRef90_P55891
UniRef50:
UniRef50_P09348
|
| {{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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