A total of fiften (15) protein sequence of Chlamydia abortus (C abortus) were retrieved from the GenBank (www.ncbi.nlm.nih.gov).The phyco-chemical properties of C abortus proteins were performed using protparam tool. The isoelectric point (pI), extinction coefficient (EC); instability index (II), aliphatic index (AI) and grand average of hydropathicity (GRAVY) were also computed. The study revealed that the pI value of C abortus protein showed that some were basic (>7) nature and acidic (<7) in nature respectively. The EC and II of protein showed that some C abortus protein have better stability which might be resistance to mutation. AI for all the protein showed that only C abortus protein with accession Number WP_072667807 showed AI > 100 which indicates thermally stable. The GRAVY of all the protein were negative (hydrophilic). The amino acid composition of C abortus proteins indicated high in serine and threonine which are hydroxyl amino acid which is non reactive and can play a role in substrate recognition.. The prediction of secondary structure was performed using SOPMA. The proteins are more of random coil structure then followed by alpha helix. Phyre2 server was used to predict the 3D structure of C abortus proteins. Molecular analysis should be carry out to substantiate this findings.
Keywords: Chlamydia abortus, Farm Animals, Mammals, Protein
