Background: Group A Streptococcus (GAS) uses several virulence factors to evade of the host’s innate immunity and establish infection. The M protein in particular has been shown to have anti-phagocytic properties. Another surface protein in M6-type GAS is streptococcal collagen-like protein 1 variant, Scl1.6. Prior studies have demonstrated that recombinant M6 and Scl1.6 bind complement factor H (CFH), leading to C3b cleavage and inhibition of complement-mediated killing. Here, we hypothesize that both M6 and Scl1.6 proteins contribute to CFH-mediated immune evasion in M6-type GAS. Methods and Results: Single M6 and Scl1.6 isogenic mutants of the M6 strain JRS4 were generated to assess loss of function. Surface M6- and Scl1.6-protein expression and CFH binding to bacterial cells was demonstrated by flow cytometry. Both mutants showed significantly decreased survival in whole blood compared to parental strain. To support these results, a heterologous host, Lactococcus lactis, was complemented in-trans for the expression of Scl1, M6, or both proteins and assayed for gain of function. Increased binding of CFH and decreased C3 deposition were detected in complemented L. lactis strains. Expression of both Scl1.6 and M6 significantly increased the survival of complemented L. lactis strains in human blood. Additionally, blocking the specific Scl1-binding site on factor H with monoclonal antibodies transiently ablates the advantage of increased survival in whole-blood. Conclusions: Our work demonstrates that CFH-binding to both Scl1.6 and M6 proteins has a functional role in complement evasion, thus, a two-component model is proposed for M6-type GAS immune evasion mediated by binding to CFH.