Acts as an extracellular and cell wall-bound hemophore; scavenges host heme and hemoglobin from the environment and also serves as a cell wall receptor for both (Probable). At low hemin (Hn) and hemoglobin (Hb) concentrations adsorbs Hn/Hb and presumably directs it to membrane transporters (Probable). Soluble Hbp2 can probably pass Hn/Hb to cell wall-anchored Hbp2, and both forms can accept Hn/Hb from Hbp1 (PubMed:25315777). May be involved in crossing the digestive barrier in infected animals (PubMed:15661014). Binds host hemin (Probable) (PubMed:21545655, PubMed:25315777). Binds host hemoglobin with affinity in the nanomolar range (PubMed:25315777). Is overexpressed in mecA, clpC and clpP mutants, suggesting the protein level is controlled by MecA, ClpC and ClpP (at protein level). Most protein is secreted (PubMed:15028680, PubMed:15661014). Cell wall attachment is iron-regulated, only occurring when iron levels are low or fur is deleted (PubMed:15661014). Cell wall-anchored protein localizes to one cell pole or laterally (PubMed:15028680). Protein does not have to be cell wall-anchored for virulence (PubMed:15028680). During exponential growth detected on the cell surface as a series of dots in a helical pattern, it is excluded from the septum (PubMed:21725001). The helical pattern of InlA does not overlap with that of InlH, InlJ or Hbp2 (PubMed:21725001). Under iron-limiting conditions accumulates at the old cell pole (PubMed:21725001). Expressed in mid-log phase, cotranscribed with lmo2184, the second gene in a possible lmo2186-lmo2180 operon (PubMed:15028680). Present in both exponential and stationary phase; more protein is expressed in log phase (at protein level) (PubMed:15028680, PubMed:16247833, PubMed:21725001). Induced under iron-deficient conditions and when fur (lmo1956, AC Q8Y5U9) is deleted (at protein level) (PubMed:15661014). Induced when bacteria are grown in human cell lines (PubMed:15661014). Each NEAT domain binds hemin, whereas only NEAT1 and NEAT3 bind hemoglobin. Moderate reduction in growth rate at 37 degrees Celsius, reduced bacterial density in stationary phase (in strain LO28); no change in bacterial adherence to Caco-2 cells (PubMed:11700342). 2-fold reduction virulence in mice (PubMed:15661014). Does not impair iron transport (PubMed:15661014, PubMed:16430693). More sensitive measurements show that disruption decreases hemin uptake at low concentrations (0.5 uM and 5 uM; at 50 uM no effect is seen) (PubMed:21545655). Decreased hemin-binding and hemin uptake by whole bacteria at low concentrations of iron (PubMed:21545655). Was originally thought to have a more extreme phenotype upon deletion; however the 100-fold reduction in virulence of the first deletion experiment, and impairment of phagosome escape seen in infected mice, is probably due to the kanamycin-cassette derivative used in that experiment.