Surfactant protein B (SP-B) is a small protein, weighing about 8 kDa. Proteins are composed of building blocks called amino acids, and SP-B is composed of 79 of them (Valine, alanine, phenylalanine, leucine, isoleucine, and tryptophan being found in the highest levels). Nine of these carry with them a positive charge, and two carry a negative charge, leaving a protein with a net (total) charge of +7. In the body, two molecules of SP-B stick together and form what is called a homodimer. These are found embedded into membranes and other lipid structures, SP-B is a highly hydrophobic, avoiding contact with water.
SP-B is the mature form of a large precursor protein called proSP-B.  Synthesized in the endoplasmic reticulum of type II pneumocytes, proSP-B weighs approximately 40 kDa and is cut down to the size of mature SP-B in the golgi apparatus through a process called post-translational modification. ProSP-B is also created in another type of lung cell called a Club cell, but these cells are unable to edit proSP-B into SP-B.
SP-B is a saposin-like protein, which is a group of related proteins known particularly for binding to membranes with negative charges and facilitating either the fusion or lysis (breaking) of the membrane.  More well known proteins in this family include saposin-C, NK-lysin, and amoebopore.