Alkaline shock proteins (ASPs) adapt to atypical conditions, which are categorized into a family of small proteins. Alkaline shock proteins are identified in many bacteria and they are involved in stress response. The molecular basis for the survival of bacteria under extreme conditions in which growth is inhibited is a question of great current interest. A preliminary study was carried out to determine residue pattern conservation among the alkaline shock proteins of enteric bacteria, responsible for extreme alkaline tolerance especially in Staphylococcus and Streptococcus. To decipher, is there any secret hidden in the alkaline shock proteins? Bioinformatics approach was used and the molecular evidence proved the relationship between Staphylococcus and Streptococcus with respect to ASP. The sequence, structure and phylogenetic analyses inferred the relationships of various bacteria with respect to the conserved motif (VDNNKAK) of ASPs. Automated subsystem functional annotation of 172 homologous ASPs was done for various bacteria. Currently the structure of the ASP is not available in the Protein Data Bank (PDB). Since the Staphylococcus species formed the root of the phylogenetic tree, the structure of the Staphylococcus aureus (strain bovine RF122) was modeled in order to understand further about the structure and mechanism.