LYSG_CORGL
ID LYSG_CORGL Reviewed; 290 AA.
AC P94632;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Lysine export transcriptional regulatory protein LysG {ECO:0000305};
GN Name=lysG {ECO:0000303|PubMed:11429454}; OrderedLocusNames=Cgl1263, cg1425;
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].
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 AS A REGULATOR.
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 [5]
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: Positively regulates the expression of the exporter LysE.
CC Induction requires the presence of a coinducer, which is either
CC intracellular L-lysine, L-arginine or L-citrulline. L-histidine also
CC acts as coinducer of lysE expression, but this amino acid is not
CC exported by LysE (PubMed:11429454, PubMed:27350619). The lysEG system
CC 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). {ECO:0000269|PubMed:11429454,
CC ECO:0000305|PubMed:27350619}.
CC -!- DISRUPTION PHENOTYPE: Deletion of lysEG decreases the extracellular
CC accumulation of L-lysine, L-arginine and L-citrulline.
CC {ECO:0000269|PubMed:27350619}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; X96471; CAA65323.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98656.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19966.1; -; Genomic_DNA.
DR RefSeq; NP_600486.1; NC_003450.3.
DR RefSeq; WP_011014240.1; NC_006958.1.
DR PDB; 6XTU; X-ray; 2.52 A; A/B=1-290.
DR PDB; 6XTV; X-ray; 3.30 A; A/B=1-290.
DR PDBsum; 6XTU; -.
DR PDBsum; 6XTV; -.
DR AlphaFoldDB; P94632; -.
DR SMR; P94632; -.
DR STRING; 196627.cg1425; -.
DR KEGG; cgb:cg1425; -.
DR KEGG; cgl:Cgl1263; -.
DR PATRIC; fig|196627.13.peg.1240; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_063829_0_1_11; -.
DR OMA; QQWKLDS; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR017685; ArgP.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR03298; argP; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..290
FT /note="Lysine export transcriptional regulatory protein
FT LysG"
FT /id="PRO_0000105668"
FT DOMAIN 1..57
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 58..82
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:6XTU"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 151..165
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:6XTU"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:6XTV"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:6XTU"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:6XTU"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:6XTU"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:6XTU"
SQ SEQUENCE 290 AA; 31388 MW; 9CE0A63F775FCB74 CRC64;
MNPIQLDTLL SIIDEGSFEG ASLALSISPS AVSQRVKALE HHVGRVLVSR TQPAKATEAG
EVLVQAARKM VLLQAETKAQ LSGRLAEIPL TIAINADSLS TWFPPVFNEV ASWGGATLTL
RLEDEAHTLS LLRRGDVLGA VTREANPVAG CEVVELGTMR HLAIATPSLR DAYMVDGKLD
WAAMPVLRFG PKDVLQDRDL DGRVDGPVGR RRVSIVPSAE GFGEAIRRGL GWGLLPETQA
APMLKAGEVI LLDEIPIDTP MYWQRWRLES RSLARLTDAV VDAAIEGLRP
