LYSG_MYCTU
ID LYSG_MYCTU Reviewed; 303 AA.
AC P9WMF5; L0TB04; P67665; Q10872;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=HTH-type transcriptional regulator LysG {ECO:0000305};
GN Name=lysG {ECO:0000303|PubMed:29049397};
GN Synonyms=argP {ECO:0000303|PubMed:20036253}; OrderedLocusNames=Rv1985c;
GN ORFNames=MTCY39.34;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=23136116; DOI=10.1128/cvi.00481-12;
RA Wang S., Chen J., Zhang Y., Diao N., Zhang S., Wu J., Lu C., Wang F.,
RA Gao Y., Shao L., Jin J., Weng X., Zhang W.;
RT "Mycobacterium tuberculosis region of difference (RD) 2 antigen Rv1985c and
RT RD11 antigen Rv3425 have the promising potential to distinguish patients
RT with active tuberculosis from M. bovis BCG-vaccinated individuals.";
RL Clin. Vaccine Immunol. 20:69-76(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=29049397; DOI=10.1371/journal.pone.0186505;
RA Schneefeld M., Busche T., Geffers R., Kalinowski J., Bange F.C.;
RT "The transcriptional regulator LysG (Rv1985c) of Mycobacterium tuberculosis
RT activates lysE (Rv1986) in a lysine-dependent manner.";
RL PLoS ONE 12:E0186505-E0186505(2017).
RN [5] {ECO:0007744|PDB:3ISP}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), DNA-BINDING, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF LYS-42; ARG-60 AND LEU-71.
RX PubMed=20036253; DOI=10.1016/j.jmb.2009.12.033;
RA Zhou X., Lou Z., Fu S., Yang A., Shen H., Li Z., Feng Y., Bartlam M.,
RA Wang H., Rao Z.;
RT "Crystal structure of ArgP from Mycobacterium tuberculosis confirms two
RT distinct conformations of full-length LysR transcriptional regulators and
RT reveals its function in DNA binding and transcriptional regulation.";
RL J. Mol. Biol. 396:1012-1024(2010).
CC -!- FUNCTION: Positively regulates the expression of the exporter LysE and
CC represses its own expression. Activity requires the presence of a
CC coinducer, lysine or histidine. Acts by binding to lysG-lysE promoter
CC region. Also up-regulates the expression of ppsB, ppsC and ppsD, by
CC binding to the upstream region of ppsB. {ECO:0000269|PubMed:29049397}.
CC -!- SUBUNIT: Homodimer (PubMed:20036253). Two types of dimers are
CC identified from the crystal packing: a DBD-type dimer, where the dimer
CC is mainly stabilized by the coiled-coil linker helices, and a RD-type
CC dimer, where RDs contact each other in an antiparallel, side-by-side
CC alignment (PubMed:20036253). {ECO:0000269|PubMed:20036253}.
CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:29049397}.
CC -!- DOMAIN: Contains an N-terminal DNA binding domain (DBD) and a C-
CC terminal regulatory domain (RD). {ECO:0000269|PubMed:20036253}.
CC -!- BIOTECHNOLOGY: A wide array of epitopes was recognized on Rv1985c in TB
CC patients. Those epitopes could specifically discriminate TB infection
CC from BCG vaccination. These results indicate that the peptide pools
CC selected from Rv1985c have the potential to diagnose TB infection by a
CC method that may be routinely used in clinical laboratories.
CC {ECO:0000269|PubMed:23136116}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44755.1; -; Genomic_DNA.
DR PIR; G70756; G70756.
DR RefSeq; NP_216501.1; NC_000962.3.
DR RefSeq; WP_003409986.1; NZ_NVQJ01000043.1.
DR PDB; 3ISP; X-ray; 2.70 A; A/B=1-303.
DR PDBsum; 3ISP; -.
DR AlphaFoldDB; P9WMF5; -.
DR SMR; P9WMF5; -.
DR STRING; 83332.Rv1985c; -.
DR PaxDb; P9WMF5; -.
DR PRIDE; P9WMF5; -.
DR GeneID; 45425964; -.
DR GeneID; 885818; -.
DR KEGG; mtu:Rv1985c; -.
DR TubercuList; Rv1985c; -.
DR eggNOG; COG0583; Bacteria.
DR OMA; QQWKLDS; -.
DR PhylomeDB; P9WMF5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MTBBASE.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:MTBBASE.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
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 PRINTS; PR00039; HTHLYSR.
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; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..303
FT /note="HTH-type transcriptional regulator LysG"
FT /id="PRO_0000105812"
FT DOMAIN 6..62
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 23..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT MUTAGEN 42
FT /note="K->E: Leads to dissociation into monomers."
FT /evidence="ECO:0000269|PubMed:20036253"
FT MUTAGEN 60
FT /note="R->E: Leads to dissociation into monomers."
FT /evidence="ECO:0000269|PubMed:20036253"
FT MUTAGEN 71
FT /note="L->W: Leads to dissociation into monomers."
FT /evidence="ECO:0000269|PubMed:20036253"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:3ISP"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:3ISP"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 155..169
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:3ISP"
FT TURN 184..189
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3ISP"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:3ISP"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:3ISP"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:3ISP"
SQ SEQUENCE 303 AA; 32837 MW; 344BDB1056207144 CRC64;
MVDPQLDGPQ LAALAAVVEL GSFDAAAERL HVTPSAVSQR IKSLEQQVGQ VLVVREKPCR
ATTAGIPLLR LAAQTALLES EALAEMGGNA SLKRTRITIA VNADSMATWF SAVFDGLGDV
LLDVRIEDQD HSARLLREGV AMGAVTTERN PVPGCRVHPL GEMRYLPVAS RPFVQRHLSD
GFTAAAAAKA PSLAWNRDDG LQDMLVRKAF RRAITRPTHF VPTTEGFTAA ARAGLGWGMF
PEKLAASPLA DGSFVRVCDI HLDVPLYWQC WKLDSPIIAR ITDTVRAAAS GLYRGQQRRR
RPG
