HTHAR_MYCTU
ID HTHAR_MYCTU Reviewed; 107 AA.
AC O53478; L0T8F6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=HTH-type transcriptional regulator Rv2034;
GN OrderedLocusNames=Rv2034;
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 FUNCTION, AND DNA-BINDING.
RX PubMed=21782791; DOI=10.1016/j.bbrc.2011.07.014;
RA Gao C.H., Yang M., He Z.G.;
RT "An ArsR-like transcriptional factor recognizes a conserved sequence motif
RT and positively regulates the expression of phoP in mycobacteria.";
RL Biochem. Biophys. Res. Commun. 411:726-731(2011).
RN [3]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, SUBUNIT, INDUCTION, AND
RP MUTAGENESIS OF ALA-32; GLU-35 AND CYS-61.
RX PubMed=22558408; DOI=10.1371/journal.pone.0036255;
RA Gao C.H., Yang M., He Z.G.;
RT "Characterization of a novel ArsR-like regulator encoded by Rv2034 in
RT Mycobacterium tuberculosis.";
RL PLoS ONE 7:E36255-E36255(2012).
CC -!- FUNCTION: Involved in the regulation of lipid metabolism and hypoxic
CC response. Positively regulates transcription of various genes, such as
CC phoP, groEL2 and dosR. Negatively regulates its own transcription. Acts
CC by binding to a specific palindromic sequence motif in promoter
CC regions. {ECO:0000269|PubMed:21782791, ECO:0000269|PubMed:22558408}.
CC -!- ACTIVITY REGULATION: DNA-binding ability is not susceptible to zinc,
CC nickel, cobalt, cadmium, lead, copper and manganese ions.
CC {ECO:0000269|PubMed:22558408}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22558408}.
CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:22558408}.
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DR EMBL; AL123456; CCP44807.1; -; Genomic_DNA.
DR PIR; A70943; A70943.
DR RefSeq; NP_216550.1; NC_000962.3.
DR RefSeq; WP_003410200.1; NZ_NVQJ01000046.1.
DR AlphaFoldDB; O53478; -.
DR SMR; O53478; -.
DR STRING; 83332.Rv2034; -.
DR PaxDb; O53478; -.
DR DNASU; 887859; -.
DR GeneID; 45426014; -.
DR GeneID; 887859; -.
DR KEGG; mtu:Rv2034; -.
DR TubercuList; Rv2034; -.
DR eggNOG; COG0640; Bacteria.
DR InParanoid; O53478; -.
DR OMA; YQQDEAW; -.
DR PhylomeDB; O53478; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01022; HTH_5; 1.
DR PRINTS; PR00778; HTHARSR.
DR SMART; SM00418; HTH_ARSR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50987; HTH_ARSR_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..107
FT /note="HTH-type transcriptional regulator Rv2034"
FT /id="PRO_0000419177"
FT DOMAIN 1..93
FT /note="HTH arsR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT DNA_BIND 33..56
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT MUTAGEN 32
FT /note="A->G: Does not bind DNA, but retains the capacity to
FT form dimers; when associated with G-35."
FT /evidence="ECO:0000269|PubMed:22558408"
FT MUTAGEN 35
FT /note="E->G: Does not bind DNA, but retains the capacity to
FT form dimers; when associated with G-32."
FT /evidence="ECO:0000269|PubMed:22558408"
FT MUTAGEN 61
FT /note="C->A: Does not bind DNA and does not form dimers."
FT /evidence="ECO:0000269|PubMed:22558408"
SQ SEQUENCE 107 AA; 11856 MW; 975FB95505F826E2 CRC64;
MSTYRSPDRA WQALADGTRR AIVERLAHGP LAVGELARDL PVSRPAVSQH LKVLKTARLV
CDRPAGTRRV YQLDPTGLAA LRTDLDRFWT RALTGYAQLI DSEGDDT