| Type | Description |
|---|---|
| Definition | CesD/SycD/LcrH family type III secretion system chaperone |
| Date | Results | Publications |
|---|---|---|
| 2014-09-13 12:14:00 | Investigated whether the tetratricopeptide repeat-like motifs in SicA are critical for transcriptional cofactor function. The canonical residues in these motifs were mutated to glutamate (SicAA44E , SicAA78E , and SicAG112E ). | 24224875 |
| 2011-03-26 10:46:00 | crystal of SicA belonged to the monoclinic space group C2, with unit-cell parameters a = 180.4, b = 94.1, c = 131.8 A, beta = 130.9 degrees | 21045315 |
| 2010-01-21 00:00:00 | SicA chaperone binds to SipB somewhere between amino acids 80 and 100 of the SipB N-terminal region. | 17768243 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
SICA_SALTY
UniprotKB:
P69066
UniParc:
UPI000005A36D
EMBL:
X73525,
U25631,
AE006468
EnsemblGenome:
STM2886
KO:
stm:STM2886
|
| Nucleutide sequences |
EMBL-CDS:
AAL21766.1,
CAA51928.1,
AAA75168.1
EnsemblGenome_TRS:
AAL21766
|
| Protein sequencees |
EnsemblGenome_PRO:
AAL21766
RefSeq:
NP_461807.1
|
| Others |
UniRef100:
UniRef100_P69064
UniRef90:
UniRef90_P69064
UniRef50:
UniRef50_P69064
|
| {{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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