Peptidoglycolipid addressing protein
The Peptidoglycolipid Addressing Protein (GAP) Family[1] is a member of the Lysine Exporter (LysE) Superfamily.[2] It is listed as item 2.A.116 in the Transporter Classification Database.The mechanism of its action is not known, but this family has been shown to be a member of the LsyE superfamily. Therefore, these proteins are most likely secondary carriers.
The proposed generalized reaction catalyzed by members of the GAP family is:
PGL (in) → PGL (outer membrane).[3]
See also
References
- ↑ Sondén, Berit; Kocíncová, Dana; Deshayes, Caroline; Euphrasie, Daniel; Rhayat, Lamya; Laval, Françoise; Frehel, Claude; Daffé, Mamadou; Etienne, Gilles (2005-10-01). "Gap, a mycobacterial specific integral membrane protein, is required for glycolipid transport to the cell surface". Molecular Microbiology. 58 (2): 426–440. doi:10.1111/j.1365-2958.2005.04847.x. ISSN 0950-382X. PMID 16194230.
- ↑ Tsu, Brian V.; Saier, Milton H. (2015-01-01). "The LysE Superfamily of Transport Proteins Involved in Cell Physiology and Pathogenesis". PloS One. 10 (10): e0137184. doi:10.1371/journal.pone.0137184. ISSN 1932-6203. PMC 4608589
. PMID 26474485. - ↑ 2.A.116 The Peptidoglycolipid Addressing Protein (GAP) Family. Transporter Classification Database.
Further reading
- Tsu, Brian V.; Saier, Milton H. "The LysE Superfamily of Transport Proteins Involved in Cell Physiology and Pathogenesis". PLOS ONE 10 (10).doi:10.1371/journal.pone.0137184. PMC 4608589.PMID 26474485.
- Seeliger, Jessica C.; Holsclaw, Cynthia M.; Schelle, Michael W.; Botyanszki, Zsofia; Gilmore, Sarah A.; Tully, Sarah E.; Niederweis, Michael; Cravatt, Benjamin F.; Leary, Julie A. (2012-03-09). "Elucidation and Chemical Modulation of Sulfolipid-1 Biosynthesis in Mycobacterium tuberculosis". Journal of Biological Chemistry 287 (11): 7990–8000. doi:10.1074/jbc.M111.315473. ISSN 0021-9258. PMC 3318749. PMID 22194604.
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