Large externalized, repeat-rich proteins are emerging as important factors in the attachment of bacteria to biotic and abiotic surfaces. An intriguing new study of the plant-associated terrestrial microbe Pseudomonas putida by Manuel Espinosa-Urgel's group that is reported in this issue of Molecular Microbiology has revealed that LapF, a huge protein (> 6000 aa) associated with the cell surface, is required for microcolony assembly from single attached cells, and in turn, formation of biofilms. Mutants defective in IapF exhibit competitive deficiencies in the rhizosphere. On both biotic and abiotic surfaces, these mutants undergo normal irreversible attachment, but cannot advance beyond this point to form multicellular clusters. The lapF phenotype is nutritionally conditional and is only manifested under a subset of growth regimes. Accordingly, lapF gene expression is controlled by the stress-responsive sigma factor RpoS and is elevated within growing microcolonies on abiotic surfaces and plant tissues. Earlier work had identified the LapA protein, another enormous cell surface protein (> 8000 aa), as a key requirement for the reversible to irreversible transition during attachment. The current findings support a model in which LapA and LapF act in a relay to drive the stable colonization of surfaces and subsequent assembly of the multicellular structures.