Haemophilus influenzae is a host-adapted pathogen that colonizes the human nasopharynx that can mediate diseases of the upper and lower respiratory tract . H. influenzae has an array of molecular mechanisms that permit growth and virulence in diverse host niches. Notably, H. influenzae can respond to exogenous, host-mediated and endogenous, i.e. metabolically produced, reactive oxygen and nitrogen stresses. Defence against these chemical insults employs enzyme-mediated detoxification processes, such as the molybdenum-dependent HITorZ. Transition metal ions serve crucial roles in bacterial growth, survival and stress response, but the majority of these mechanisms in H. influenzae remain to be determined. Bioinformatic analyses of H. influenzae 2019 revealed that it encoded two ATP-binding cassette (ABC) transporter solute binding proteins (SBPs) that belonged to the cluster A-I subgroup. Primary sequence analyses suggested that these were orthologs of a manganese-specific (locus tag: C645_00940) and zinc-specific (locus tag: C645_02340) SBPs. Given the central role of manganese in metabolism and resistance to oxidative stress we investigated the biochemical and biophysical properties of C645_00940. We combined recombinant protein purification with in vitro metal binding assays to show that C645_00940 was a manganese-binding SBP. Building on this finding, the gene was renamed as HIPsaA due to the functional and structural similarity to Streptococcus pneumoniae PsaA. Collectively, this work provides insight into manganese acquisition in H. influenzae and the contribution of this transition metal ion to bacterial virulence.