VIRS_MYCTU
ID VIRS_MYCTU Reviewed; 340 AA.
AC P9WMJ3; L0TBI3; O53299; Q06861;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=HTH-type transcriptional regulator VirS;
DE AltName: Full=Virulence-regulating protein VirS;
GN Name=virS; OrderedLocusNames=Rv3082c; ORFNames=MTV013.03c;
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 [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8472958; DOI=10.1016/0378-1119(93)90607-5;
RA Gupta S., Tyagi A.K.;
RT "Sequence of a newly identified Mycobacterium tuberculosis gene encoding a
RT protein with sequence homology to virulence-regulating proteins.";
RL Gene 126:157-158(1993).
RN [2]
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 [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14568148; DOI=10.1016/s0378-1097(03)00648-7;
RA Singh A., Jain S., Gupta S., Das T., Tyagi A.K.;
RT "mymA operon of Mycobacterium tuberculosis: its regulation and importance
RT in the cell envelope.";
RL FEMS Microbiol. Lett. 227:53-63(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=Erdman;
RX PubMed=15937179; DOI=10.1128/jb.187.12.4173-4186.2005;
RA Singh A., Gupta R., Vishwakarma R.A., Narayanan P.R., Paramasivan C.N.,
RA Ramanathan V.D., Tyagi A.K.;
RT "Requirement of the mymA operon for appropriate cell wall ultrastructure
RT and persistence of Mycobacterium tuberculosis in the spleens of guinea
RT pigs.";
RL J. Bacteriol. 187:4173-4186(2005).
RN [5]
RP PHOSPHORYLATION, AND DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19251699; DOI=10.1074/jbc.m808705200;
RA Kumar P., Kumar D., Parikh A., Rananaware D., Gupta M., Singh Y.,
RA Nandicoori V.K.;
RT "The Mycobacterium tuberculosis protein kinase K modulates activation of
RT transcription from the promoter of mycobacterial monooxygenase operon
RT through phosphorylation of the transcriptional regulator VirS.";
RL J. Biol. Chem. 284:11090-11099(2009).
CC -!- FUNCTION: Regulates the expression of the mymA operon (Rv3083-Rv3089).
CC {ECO:0000269|PubMed:14568148}.
CC -!- INDUCTION: Induced at acidic pH. Negatively autoregulated.
CC {ECO:0000269|PubMed:14568148}.
CC -!- PTM: Phosphorylated by PknK. Phosphorylation increases affinity for the
CC mymA promoter. {ECO:0000269|PubMed:19251699}.
CC -!- DISRUPTION PHENOTYPE: Mutant displays altered colony morphology and
CC cell wall structure, reduced contents and altered composition of
CC mycolic acids along with the accumulation of saturated C24 and C26
CC fatty acids, and enhanced susceptibility to antibiotics, detergents and
CC acidic pH. Also impairs ability to survive in activated macrophages,
CC but not in resting macrophages. {ECO:0000269|PubMed:14568148,
CC ECO:0000269|PubMed:15937179}.
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DR EMBL; X68281; CAA48342.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45891.1; -; Genomic_DNA.
DR PIR; F70852; F70852.
DR RefSeq; NP_217598.1; NC_000962.3.
DR RefSeq; WP_003416068.1; NZ_NVQJ01000011.1.
DR AlphaFoldDB; P9WMJ3; -.
DR SMR; P9WMJ3; -.
DR STRING; 83332.Rv3082c; -.
DR PaxDb; P9WMJ3; -.
DR DNASU; 888657; -.
DR GeneID; 888657; -.
DR KEGG; mtu:Rv3082c; -.
DR TubercuList; Rv3082c; -.
DR eggNOG; COG2207; Bacteria.
DR OMA; LMVGESW; -.
DR PhylomeDB; P9WMJ3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0071468; P:cellular response to acidic pH; IEP:MTBBASE.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MTBBASE.
DR InterPro; IPR032687; AraC-type_N.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR Pfam; PF12625; Arabinose_bd; 1.
DR Pfam; PF12833; HTH_18; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..340
FT /note="HTH-type transcriptional regulator VirS"
FT /id="PRO_0000194592"
FT DOMAIN 236..334
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 254..275
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 301..324
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT CONFLICT 21..22
FT /note="EL -> DV (in Ref. 1; CAA48342)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..163
FT /note="PQAR -> RSG (in Ref. 1; CAA48342)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> R (in Ref. 1; CAA48342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37789 MW; D3EB1B640D3BEF75 CRC64;
MELGSLIRAT NLWGYTDLMR ELGADPLPFL RRFDIPPGIE HQEDAFMSLA GFVRMLEASA
AELDCPDFGL RLARWQGLGI LGPVAVIARN AATLFGGLEA IGRYLYVHSP ALTLTVSSTT
ARSNVRFGYE VTEPGIPYPL QGYELSMANA ARMIRLLGGP QARARVFSFR HAQLGTDAAY
REALGCTVRF GRTWCGFEVD HRLAGRPIDH ADPETKRIAT KYLESQYLPS DATLSERVVG
LARRLLPTGQ CSAEAIADQL DMHPRTLQRR LAAEGLRCHD LIERERRAQA ARYLAQPGLY
LSQIAVLLGY SEQSALNRSC RRWFGMTPRQ YRAYGGVSGR