The primary sequence length of the protein is 272 amino acids, it also includes the signal peptide of 20-mer residues.

The ESPript method is a qualitative method of studying conservation. From the MSA generated we observed that active site residues and standard class A elements (SXXK, SDN, KXG), and loops to be conserved in all the variants of cepA Beta-lactamase, they are: SVFK(70-73), SDN(130-132), KTG(234-236). The omega loop, although present in CepA has a different set of amino acid residues as compared to other prevalently studied Class A Beta-lactamases such as TEM, SHV, and CTX-M and is similar to PER-1. A single variable residue is observed among the common conserved regions at position 171. It is part of the omega loop, 14 of the 23 residues have a glutamate residue instead of lysine. .