Previously we have reported on a cell surface collagen-like protein, called SclC, from Streptococcus equi subspecies equi. In the present study we show that this protein is a member of a family of seven collagen-like proteins, called SclC-SclI in this subspecies. All proteins contain an N-terminal signal sequence, followed by a unique non-repetitive region called A, a highly repetitive collagen-like region (CL) consisting of Glycine-Xaa-Yaa-triplet repeats. Following the CL-region a C-terminal proline-rich putative wall spanning region (W) preceding an LPXTG-motif and a hydrophobic transmembrane region (M) are found, typical features of cell surface exposed proteins in Gram-positive bacteria. The nucleotide and amino acid sequences, were analysed to investigate the similarities between them, and recombinant proteins encoding different domains (A- and CL-regions) were expressed and purified. Although the novel collagen-like proteins display differences in amino acid sequences, affinity purified antibodies against SclC were found to cross react with the other members of the novel collagen-like proteins. Furthermore, in sera from horses previously diagnosed having strangles, antibodies against these proteins were detected suggesting that these proteins are expressed during the infection.