| Type | Description |
|---|---|
| Definition | flagellar biosynthesis protein FliT |
| Date | Results | Publications |
|---|---|---|
| 2018-01-27 11:44:00 | The solution structure of the FliT chaperone in the free state and in complex with FliD and the flagellar ATPase FliI has been determined. | 27528687 |
| 2015-02-14 14:00:00 | Data indicate that FliT and ClpXP work concertedly to repress FlhD4C2 activity by enhanced degradation of FlhC subunit. | 25278020 |
| 2012-04-14 11:49:00 | The C-terminal alpha4 helix of FliT suppressed the interaction with FliI. | 22111876 |
| 2010-01-21 00:00:00 | We conclude that FliT acts as an anti-FlhD(2)C(2) factor, which binds to FlhD(2)C(2) through interaction with the FlhC subunit and inhibits its binding to the class 2 promoter | 16952964 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
FLIT_SALTY
UniprotKB:
P0A1N2
UniParc:
UPI0000059CB9
EMBL:
L01643,
AE006468,
M85241
EnsemblGenome:
STM1962
KO:
stm:STM1962
|
| Nucleutide sequences |
EMBL-CDS:
AAA27078.1,
AAL20874.1,
AAA27109.1
EnsemblGenome_TRS:
AAL20874
|
| Protein sequencees |
EnsemblGenome_PRO:
AAL20874
RefSeq:
NP_460915.1
|
| Others |
UniRef100:
UniRef100_B5F2S6
UniRef90:
UniRef90_B5F2S6
UniRef50:
UniRef50_B5F2S6
|
| {{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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