LYSE_CORGL
ID LYSE_CORGL Reviewed; 233 AA.
AC P94633;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Lysine exporter LysE {ECO:0000305};
GN Name=lysE {ECO:0000303|PubMed:8971704}; OrderedLocusNames=Cgl1262, cg1424;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=R127;
RX PubMed=8971704; DOI=10.1046/j.1365-2958.1996.01527.x;
RA Vrljic M.M., Sahm H., Eggeling L.;
RT "A new type of transporter with a new type of cellular function: L-lysine
RT export from Corynebacterium glutamicum.";
RL Mol. Microbiol. 22:815-826(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=1935969; DOI=10.1111/j.1432-1033.1991.tb16353.x;
RA Broeer S., Kraemer R.;
RT "Lysine excretion by Corynebacterium glutamicum. 1. Identification of a
RT specific secretion carrier system.";
RL Eur. J. Biochem. 202:131-135(1991).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1657604; DOI=10.1111/j.1432-1033.1991.tb16354.x;
RA Broeer S., Kraemer R.;
RT "Lysine excretion by Corynebacterium glutamicum. 2. Energetics and
RT mechanism of the transport system.";
RL Eur. J. Biochem. 202:137-143(1991).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10943564;
RA Vrljic M., Garg J., Bellmann A., Wachi S., Freudl R., Malecki M.J.,
RA Sahm H., Kozina V.J., Eggeling L., Saier M.H. Jr., Eggeling L.,
RA Saier M.H. Jr.;
RT "The LysE superfamily: topology of the lysine exporter LysE of
RT Corynebacterium glutamicum, a paradyme for a novel superfamily of
RT transmembrane solute translocators.";
RL J. Mol. Microbiol. Biotechnol. 1:327-336(1999).
RN [7]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11429454; DOI=10.1099/00221287-147-7-1765;
RA Bellmann A., Vrljic M., Patek M., Sahm H., Kraemer R., Eggeling L.;
RT "Expression control and specificity of the basic amino acid exporter LysE
RT of Corynebacterium glutamicum.";
RL Microbiology 147:1765-1774(2001).
RN [8]
RP FUNCTION IN D-LYSINE EXPORT.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=21257776; DOI=10.1128/jb.01295-10;
RA Staebler N., Oikawa T., Bott M., Eggeling L.;
RT "Corynebacterium glutamicum as a host for synthesis and export of D-Amino
RT Acids.";
RL J. Bacteriol. 193:1702-1709(2011).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=27350619; DOI=10.1007/s00253-016-7695-1;
RA Lubitz D., Jorge J.M., Perez-Garcia F., Taniguchi H., Wendisch V.F.;
RT "Roles of export genes cgmA and lysE for the production of L-arginine and
RT L-citrulline by Corynebacterium glutamicum.";
RL Appl. Microbiol. Biotechnol. 100:8465-8474(2016).
CC -!- FUNCTION: Catalyzes the efflux of L-lysine (PubMed:8971704,
CC PubMed:1657604, PubMed:1935969, PubMed:27350619). Can also export L-
CC arginine and L-citrulline (PubMed:11429454, PubMed:27350619). The lysEG
CC system prevents bacteriostasis due to elevated L-lysine or L-arginine
CC concentrations that arise during growth in the presence of peptides or
CC in mutants possessing a deregulated biosynthesis pathway
CC (PubMed:11429454). In vitro, can also export D-lysine during
CC biotechnological production of D-amino acids (PubMed:21257776).
CC {ECO:0000269|PubMed:11429454, ECO:0000269|PubMed:1657604,
CC ECO:0000269|PubMed:1935969, ECO:0000269|PubMed:21257776,
CC ECO:0000269|PubMed:27350619, ECO:0000269|PubMed:8971704}.
CC -!- ACTIVITY REGULATION: Transport process is modulated by three forces:
CC the membrane potential, the chemical potential of lysine, and the
CC proton gradient (PubMed:1657604). Strongly inhibited by CCCP and
CC valinomycin (PubMed:1657604). {ECO:0000269|PubMed:1657604}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:10943564}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Although six hydrophobic domains were identified
CC based on hydropathy analysis, only five transmembrane spanning helices
CC appear to be present. The additional hydrophobic segment may dip into
CC the membrane or be surface localized. {ECO:0000269|PubMed:10943564}.
CC -!- INDUCTION: Positively regulated by LysG. {ECO:0000269|PubMed:11429454}.
CC -!- DISRUPTION PHENOTYPE: Null mutant is unable to excrete L-lysine
CC (PubMed:8971704). Deletion of lysEG decreases the extracellular
CC accumulation of L-lysine, L-arginine and L-citrulline
CC (PubMed:27350619). {ECO:0000269|PubMed:27350619,
CC ECO:0000269|PubMed:8971704}.
CC -!- SIMILARITY: Belongs to the LysE/ArgO transporter (TC 2.A.75) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98655.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X96471; CAA65324.2; -; Genomic_DNA.
DR EMBL; BA000036; BAB98655.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927151; CAF19965.1; -; Genomic_DNA.
DR RefSeq; NP_600485.1; NC_003450.3.
DR AlphaFoldDB; P94633; -.
DR SMR; P94633; -.
DR STRING; 196627.cg1424; -.
DR TCDB; 2.A.75.1.1; the l-lysine exporter (lyse) family.
DR KEGG; cgb:cg1424; -.
DR KEGG; cgl:Cgl1262; -.
DR PATRIC; fig|196627.13.peg.1239; -.
DR eggNOG; COG1279; Bacteria.
DR HOGENOM; CLU_087840_0_0_11; -.
DR OMA; FARPRAW; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR001123; LeuE-type.
DR InterPro; IPR004777; Lys/arg_exporter.
DR PANTHER; PTHR30086; PTHR30086; 2.
DR Pfam; PF01810; LysE; 1.
DR TIGRFAMs; TIGR00948; 2a75; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..233
FT /note="Lysine exporter LysE"
FT /id="PRO_0000204157"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10943564"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..65
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10943564"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10943564"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..176
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10943564"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10943564"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 25082 MW; F5FD9B1ACAD11D13 CRC64;
MEIFITGLLL GASLLLSIGP QNVLVIKQGI KREGLIAVLL VCLISDVFLF IAGTLGVDLL
SNAAPIVLDI MRWGGIAYLL WFAVMAAKDA MTNKVEAPQI IEETEPTVPD DTPLGGSAVA
TDTRNRVRVE VSVDKQRVWV KPMLMAIVLT WLNPNAYLDA FVFIGGVGAQ YGDTGRWIFA
AGAFAASLIW FPLVGFGAAA LSRPLSSPKV WRWINVVVAV VMTALAIKLM LMG
