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2.A.75 The L-Lysine Exporter (LysE) Family

Two members of the LysE family (LysE of Corynebacterium glutamicum and ArgO of E. coli) have been functionally characterized, but functionally uncharacterized homologues are encoded within the genomes of many bacteria including Mycobacterium tuberculosis, Bacillus subtilis, Aeromonas salmonicida, Helicobacter pylori, Vibrio cholerae and Yersinia pestis. Thus, LysE family members are found widely distributed in Gram-negative and Gram-positive bacteria. These proteins are 190-240 amino acyl residues in length and possess six hydrophobic regions. PhoA fusion analyses of LysE of C. glutamicum provided evidence for a 5 transmembrane α-helical spanner (TMS) typology with the N-terminus inside and the C-terminus outside (Vrljic et al., 1999). However, some evidence suggests a 6 TMS topology (R. Kramer, personal communication).

LysE appears to catalyze unidirectional efflux of L-lysine (and other basic amino acids such as L-arginine), and it provides the sole route for L-lysine excretion. The energy source is believed to be the proton motive force (H+ antiport). The E. coli ArgO homologue effluxes arginine and possibly lysine and canavanine as well (Nandineni and Gowrishankar, 2004).

Early studies showed that the LysE family is related to the RhtB family (TC #2.A.76) as well as the CadD family (TC #2.A.77) based both on the similar sizes and topologies of their members and on PSI-BLAST results (Vrljic et al., 1999). Thus, three families comprise the LysE superfamily, the members of which are restricted to bacteria and archaea.

The generalized transport reaction for LysE is:

Lysine (in) + [nH+ (out) or nOH- (in)] Lysine (out) + [nH+ (in) or nOH- (out)]

This family belongs to the: LysE Superfamily.

References associated with 2.A.75 family:

Aleshin, V.V., N.P. Zakataeva, and V.A. Livshits, (1999). A new family of amino-acid-efflux proteins. Trends Biochem. Sci. 24: 133-135. 10322417
Bröer, S. and R. Krämer. (1991a). Lysine excretion by Corrynebacterium glutamicum. 1. Identification of a specific secretion carrier system. Eur. J. Biochem. 202: 131-135.
Bröer, S. and R. Krämer. (1991b). Lysine excretion by Corynebacterium glutamicum. 2. Energetics and mechanism of the transport system. Eur. J. Biochem. 202: 137-143.
Cai, T., W. Cai, J. Zhang, H. Zheng, A.M. Tsou, L. Xiao, Z. Zhong, and J. Zhu. (2009). Host legume-exuded antimetabolites optimize the symbiotic rhizosphere. Mol. Microbiol. 73: 507-517. 19602148
García-Mesa, Y., J. Feito, P. Cuendias, J. García-Piqueras, A. Germanà, O. García-Suárez, B. Martín-Biedma, and J.A. Vega. (2022). The acquisition of mechanoreceptive competence by human digital Merkel cells and sensory corpuscles during development: An immunohistochemical study of PIEZO2. Ann Anat 243: 151953. [Epub: Ahead of Print] 35523396
Lubitz, D., J.M. Jorge, F. Pérez-García, H. Taniguchi, and V.F. Wendisch. (2016). Roles of export genes cgmA and lysE for the production of L-arginine and L-citrulline by Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 100: 8465-8474. 27350619
Marbaniang, C.N. and J. Gowrishankar. (2012). Transcriptional cross-regulation between Gram-negative and gram-positive bacteria, demonstrated using ArgP-argO of Escherichia coli and LysG-lysE of Corynebacterium glutamicum. J. Bacteriol. 194: 5657-5666. 22904281
Nandineni, M.R. and J. Gowrishankar. (2004). Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli. J. Bacteriol. 186: 3539-3546. 15150242
Pathania, A. and A.A. Sardesai. (2015). Distinct Paths for Basic Amino Acid Export in Escherichia coli: YbjE (LysO) Mediates Export of l-Lysine. J. Bacteriol. 197: 2036-2047. 25845847
Pathania, A., A.K. Gupta, S. Dubey, B. Gopal, and A.A. Sardesai. (2016). The Topology of the l-Arginine Exporter ArgO Conforms to an Nin-Cout Configuration in Escherichia coli: Requirement for the Cytoplasmic N-Terminal Domain, Functional Helical Interactions, and an Aspartate Pair for ArgO Function. J. Bacteriol. 198: 3186-3199. 27645388
Stäbler, N., T. Oikawa, M. Bott, and L. Eggeling. (2011). Corynebacterium glutamicum as a host for synthesis and export of D-Amino Acids. J. Bacteriol. 193: 1702-1709. 21257776
Vrljic, M., H. Sahm, and L. Eggeling. (1996). A new type of transporter with a new type of cellular function: L-lysine export from Corynebacterium glutamicum. Mol. Microbiol. 22: 815-826. 8971704
Vrljic, M., J. Garg, A. Bellmann, S. Wachi, R. Freudl, M.J. Malecki, H. Sahm, V.J. Kozina, L. Eggeling, and M.H. Saier, Jr. (1999). The LysE superfamily: topology of the lysine exporter LysE of Corynebacterium glutamicum, a paradigm for a novel superfamily of transmembrane solute translocators. J. Mol. Microbiol. Biotechnol. 1: 327-336. 10943564