I'm afraid that each protein has its particular half life, and it depend on the physiological state of the cell, nutrient availability, strain and many other factors. The best way to know is by experimental measurement of the half-life in a given situation/conditions. The data about this are scarce but you can look on PUBMED for each protein, case to case. Here you have more recent information: http://www.mrc-lmb.cam.ac.uk/genomes/madanm/janga_mbs.pdf. Good luck.   

for in vitro, you can try expasy protparam. not sure about in vivo...may look for specific papers

Dear Santosh, 

The experimental avg. half-life for bacterial proteins is ~20 h. This is published here 

Koch AL, Levy HR. (1955). Protein turnover in growing cultures of Escherichia coli. J Biol Chem 217: 947–958.

Mandelstam J. (1957). Turnover of protein in growing and non-growing populations of Escherichia coli. Biochem J 6: 110–119.

Borek E, Ponticorvo L, Rittenberg D. (1958). Protein turnover in microorganisms. Proc Natl Acad Sci USA 44: 369–374.

Hope this is helpful.

not sure thanks

I'm afraid that each protein has its particular half life, and it depend on the physiological state of the cell, nutrient availability, strain and many other factors. The best way to know is by experimental measurement of the half-life in a given situation/conditions. The data about this are scarce but you can look on PUBMED for each protein, case to case. Here you have more recent information: http://www.mrc-lmb.cam.ac.uk/genomes/madanm/janga_mbs.pdf. Good luck.   

Thanks Andaleeb and Kamlesh.. However I am looking for in vivo half lives of a few E. coli proteins... As rightly mentioned by Alexandro, each protein would have a different half life.. I was looking for any database or high-throughput study having info on each protein.

Thanks Alexandro for the link. It was really helpful.

try looking on PortEco site - there are many databases with info there.  Not sure if protein degradation data are posted there - you might give them feedback if you can't find it

http://www.porteco.org/help/general.jsp

I am not aware of any high throughput study of protein half lives. Measuring half lives involves pulse-labeling with a radioactive amino acids (S35 Methionine, typically), then blocking the protein synthesis + adding cold methionine at time=0, and following the protein levels over a period of time (say each 10-30 minutes). Some proteins have a very short half-life and others are very stable, so you have to find the right time frame for each case. All this requires specific antibodies for each of these proteins to detect them in the total extract, typically by immunoprecipitation. I don't see how this can be predicted by computational methods - it depends on protein partners, compartment and conditions as A.Rodriguez Rojas rightfully pointed out.

A more correct approach would be to clone the gene coding for your protein of interest under the T7 promoter in bacterial cells that express T7-RNA polymerase, block RNA transcription from other promoters by Rifampicin (blocks the E. coli RNApol but not the T7 one), add 35S-Met, incubate for 30 min or so, wash the labeled Met and add regular methionin. Google "Pulse-Chase" and E. coli

And if someone have access to LC-MS-MS, and some extra money, an isotopic (SILAC) pulse-chase could probebly be done...

Yoram

See the linked paper. This is the only work I've found that studies this question at the proteomic level. For fast-growing E. coli, the rate of effective degradation by dilution is quite similar to delays associated with transcription and translation, so regulated degradation is not so important.

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2984242/

first of all decide a few proteins which you may be interesed to study. Then first of go to PubMed site and type your question in the query box and see if you get the answers which satisfy you (it should). If not then you may use PDB databases like Swissprot etc. to look for the answer to your question.

There should not be any recent works on this where you can get information about specific proteins. Some older works have shown that most protein half-lives in E. coli are long compared to cell doubling times at least in steady state cultures.

Calandruccio and Larrabee 1981; Nath and Koch 1970; St. John et al. 1979

SILAC pulse labelling +LC MS/MS in E. coli has not been done as far as I am aware. There is data for L.Lactis, though: 

http://www.ncbi.nlm.nih.gov/pubmed/24739216