Klebsiella pneumoniae is a Gram-negative opportunistic pathogen of humans and is recognised for causing urinary tract infections, pneumonia and septicaemia in immuno-compromised individuals. Treatment of these infections can be difficult due to the emergence of multi-drug resistant K. pneumoniae strains. The expression of a thick polysaccharide capsule contributes to antibiotic resistance and resistance to phagocytosis and is considered the major virulence factor of K. pneumoniae. Some hyper-mucoid K. pneumoniae isolates encode the ‘regulator of mucoid phenotype’ (RMP) genes and over-expresses capsule polysaccharide (CPS). However it is becoming evident that capsule-overexpression is not always advantageous to bacterial survival and requires a degree of co-regulation. Our research shows that K. pneumoniae as a species seldom encode type V secretion proteins. These proteins are implicated with pathogenicity in numerous other groups of bacteria, including diverse species in the Enterbacteriace to which K. pneumoniae belongs. Type V secretion proteins are sub-categorised as i) Auto-Transporters (ATs) ii) Two-partner Secretion Systems (TSS), iii) Trimeric Auto-Transporter adhesins (TAA), and (iv) intimins/invasins. As with other type V secretion system proteins, AT function is dictated by the passenger domain and this must be translocated through the β-barrel domain of the AT out onto the surface of the bacteria. Two characteristic ATs: one with a Phospholipase B passenger domain and the other with a Protease passenger domain were transformed into a K. pneumoniae B5055 expression model. Initial data suggests that the presence of a thick capsule prevents K. pneumoniae from secreting functional protein effectively.