General rule information
[?]
Accession |
PRU00422 |
Dates |
6-APR-2005 (Created) 21-NOV-2019 (Last updated, Version 17) |
Predictors |
PROSITE; PS51099; PTS_EIIB_TYPE_2
|
Name |
PTS EIIB type-2 domain |
Function |
Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. |
Propagated annotation
[?]
case (<OC:Bacteria> or <OC:Archaea>) and <Feature:PS51099:8=C>
Domain |
The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain. |
end case
case (<OC:Bacteria> or <OC:Archaea>) and <Feature:PS51099:8=C>
GO:0016740; Molecular function: transferase activity.
end case
From: PS51099 |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
DOMAIN
|
|
from
|
|
to
|
|
PTS EIIB type-2 #
|
|
|
|
|
|
|
MOD_RES
|
|
8
|
|
8
|
|
Phosphocysteine; by EIIA
|
|
|
|
C
|
|
|
Additional information
[?]
Warning |
This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, CC, FT DOMAIN AND CC CATALYTIC ACTIVITY. |
Size range |
98 amino acids |
Related rules |
none |
Repeats |
1-2 |
Topology |
Undefined |
Example |
P20966 (PTFBC_ECOLI) |
Scope |
Bacteria
Archaea |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see
prosite_license.html.
UniProtKB rule member sequences
[?]