Protein Family Models

This domain often occurs confers as the leader peptidase domain of transporter subunits involved in cleaving peptides or proteins, such as bacteriocins with a double-glycine type leader peptide, during export.

Date:

2024-10-16

ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains. [1]. 1864505. Homology between proteins controlling Streptomyces fradiae tylosin resistance and ATP-binding transport. Rosteck PR Jr, Reynolds PA, Hershberger CL;. Gene 1991;102:27-32. [2]. 1977073. Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Blight MA, Holland IB;. Mol Microbiol 1990;4:873-880. [3]. 2229036. Binding protein-dependent transport systems. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP;. J Bioenerg Biomembr 1990;22:571-592. [4]. 9872322. Crystal structure of the ATP-binding subunit of an ABC transporter. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH;. Nature 1998;396:703-707. (from Pfam)

Date:

2024-10-16

Members of this family, found in Mycoplasmopsis bovis and related species, contain an N-terminal C39-family cysteine peptidase domain, followed by an ABC transporter permease domain and an ABC transporter ATP-binding cassette domain. This architecture is typical of transporters that combine cleavage of a bacteriocin or peptide pheromone precursor at a Gly-Gly dipeptide site with export from the cell. However, so far no peptide precursor has been detected near members of this family.

Date:

2024-06-02