Difference between revisions of "Protein modification"
(→Protein kinases) |
|||
| (5 intermediate revisions by the same user not shown) | |||
| Line 18: | Line 18: | ||
=== Protein maturation === | === Protein maturation === | ||
* ''[[ctaG]]'' | * ''[[ctaG]]'' | ||
| − | * ''[[ | + | * ''[[defA]]'' |
* ''[[lgt]]'' | * ''[[lgt]]'' | ||
* ''[[map]]'' | * ''[[map]]'' | ||
* ''[[yflG]]'' | * ''[[yflG]]'' | ||
| − | |||
=== Protein kinases === | === Protein kinases === | ||
| Line 29: | Line 28: | ||
* ''[[citS]]'' | * ''[[citS]]'' | ||
* ''[[comP]]'' | * ''[[comP]]'' | ||
| + | * ''[[cotH]]'' | ||
* ''[[cssS]]'' | * ''[[cssS]]'' | ||
* ''[[dctS]]'' | * ''[[dctS]]'' | ||
| Line 126: | Line 126: | ||
==Key Reviews== | ==Key Reviews== | ||
| − | + | <pubmed> 21372323 20487279 21239213 25625314 25852656</pubmed> | |
| − | <pubmed> 21372323 20487279 </pubmed> | ||
=Back to [[categories]]= | =Back to [[categories]]= | ||
Latest revision as of 17:00, 19 May 2016
| Parent categories | |
| Neighbouring categories |
|
| Related categories | |
Genes in this functional category
Protein maturation
Protein kinases
- bceS
- cheA
- citS
- comP
- cotH
- cssS
- dctS
- degS
- desK
- epsA
- epsB
- glnK
- hprK
- kinA
- kinB
- kinC
- kinD
- kinE
- liaS
- lytS
- malK
- mcsB
- natK
- phoR
- prkC
- prkD
- psdS
- ptkA
- resE
- rsbT
- rsbW
- spoIIAB
- tkmA
- walK
- ybdK
- ycbM
- yclK
- ydfH
- yesM
- yfiJ
- yhcY
- ykoH
- yrkQ
- yvfT
- yvrG
- ywpD
- yxdK
- yxjM
Protein kinase/ based on similarity
Protein phosphatases
- cheC
- phrI
- phrK
- prpC
- prpE
- ptpZ
- rapA
- rapB
- rapC
- rapD
- rapE
- rapF
- rapG
- rapH
- rapI
- rapJ
- rapK
- rsbP
- rsbU
- rsbX
- spo0E
- spoIIE
- yfkJ
- yisI
- ywlE
Protein acetylases/ deacetylases
Protein acetylase/ deacetylase/ based on similarity
Protein deaminase
Protein modification/ other
Key Reviews
Vu Van Loi, Martina Rossius, Haike Antelmann
Redox regulation by reversible protein S-thiolation in bacteria.
Front Microbiol: 2015, 6;187
[PubMed:25852656]
[WorldCat.org]
[DOI]
(P e)
Jonathan Dworkin
Ser/Thr phosphorylation as a regulatory mechanism in bacteria.
Curr Opin Microbiol: 2015, 24;47-52
[PubMed:25625314]
[WorldCat.org]
[DOI]
(I p)
Sandro F F Pereira, Lindsie Goss, Jonathan Dworkin
Eukaryote-like serine/threonine kinases and phosphatases in bacteria.
Microbiol Mol Biol Rev: 2011, 75(1);192-212
[PubMed:21372323]
[WorldCat.org]
[DOI]
(I p)
Sandy Thao, Jorge C Escalante-Semerena
Control of protein function by reversible Nɛ-lysine acetylation in bacteria.
Curr Opin Microbiol: 2011, 14(2);200-4
[PubMed:21239213]
[WorldCat.org]
[DOI]
(I p)
Linda I Hu, Bruno P Lima, Alan J Wolfe
Bacterial protein acetylation: the dawning of a new age.
Mol Microbiol: 2010, 77(1);15-21
[PubMed:20487279]
[WorldCat.org]
[DOI]
(I p)
