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2.A.114 The Peptide Transporter Carbon Starvation CstA (CstA) Family

The CstA family consists of proteins from bacteria, and archaea. These proteins are of various sizes and topologies. For example, CstA of E. coli has 701 aas with 18 putative TMSs. It has a long N-terminal CstA domain and a short C-terminal DUF4161 domain. This protein is encoded by a carbon starvation inducible gene cstA that is under cyclic AMP-CRP control. Circumstantial evidence suggested that it may be a peptide transporter (Schultz and Matin, 1991). A Campylobacter jejuni homologue has been shown to transport di- and tripeptides (see TC# 2.A.114.1.5) (Rasmussen et al., 2013).

This family belongs to the: APC Superfamily.

References associated with 2.A.114 family:

Behr, S., L. Fried, and K. Jung. (2014). Identification of a novel nutrient-sensing histidine kinase/response regulator network in Escherichia coli. J. Bacteriol. 196: 2023-2029. 24659770
Kraxenberger, T., L. Fried, S. Behr, and K. Jung. (2012). First insights into the unexplored two-component system YehU/YehT in Escherichia coli. J. Bacteriol. 194: 4272-4284. 22685278
Rasmussen, J.J., C.S. Vegge, H. Frøkiær, R.M. Howlett, K.A. Krogfelt, D.J. Kelly, and H. Ingmer. (2013). Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells. J. Med. Microbiol. 62: 1135-1143. 23682166
Schultz, J.E. and A. Matin. (1991). Molecular and functional characterization of a carbon starvation gene of Escherichia coli. J. Mol. Biol. 218: 129-140. 1848300