ID   DOST_MYCTO              Reviewed;         573 AA.
AC   P9WGK0; L0TB49; O53473; Q7D7L6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Oxygen sensor histidine kinase response regulator DosT {ECO:0000305};
GN   Name=dosT; OrderedLocusNames=MT2086;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Interacts with the two-component regulatory system DevR/DevS
CC       (DosR/DosS) involved in onset of the dormancy response. Required for
CC       full induction of the DevR (DosR) regulon; required during early
CC       adaptation to anaerobiosis, to start induction of the DevR regulon (By
CC       similarity). May act as a direct hypoxia/oxygen sensor (By similarity).
CC       May be the secondary sensor for CO (By similarity). Donates a phosphate
CC       group to DevR (DosR) (By similarity). {ECO:0000250|UniProtKB:P9WGK1}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WGK1};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P9WGK1};
CC       Note=Binds 1 heme group per monomer. {ECO:0000250|UniProtKB:P9WGK1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WGK1}.
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DR   EMBL; AE000516; AAK46365.1; -; Genomic_DNA.
DR   PIR; B70942; B70942.
DR   RefSeq; WP_003899138.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGK0; -.
DR   SMR; P9WGK0; -.
DR   EnsemblBacteria; AAK46365; AAK46365; MT2086.
DR   KEGG; mtc:MT2086; -.
DR   PATRIC; fig|83331.31.peg.2250; -.
DR   HOGENOM; CLU_034370_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme; Iron; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW   Repeat; Transferase; Two-component regulatory system.
FT   CHAIN           1..573
FT                   /note="Oxygen sensor histidine kinase response regulator
FT                   DosT"
FT                   /id="PRO_0000428348"
FT   DOMAIN          61..198
FT                   /note="GAF 1"
FT   DOMAIN          229..366
FT                   /note="GAF 2"
FT   DOMAIN          380..573
FT                   /note="Histidine kinase"
FT   BINDING         147
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         392
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   573 AA;  62169 MW;  83875E7C555D156E CRC64;
     MTHPDRANVN PGSPPLRETL SQLRLRELLL EVQDRIEQIV EGRDRLDGLI DAILAITSGL
     KLDATLRAIV HTAAELVDAR YGALGVRGYD HRLVEFVYEG IDEETRHLIG SLPEGRGVLG
     ALIEEPKPIR LDDISRHPAS VGFPLHHPPM RTFLGVPVRI RDEVFGNLYL TEKADGQPFS
     DDDEVLVQAL AAAAGIAVDN ARLFEESRTR EAWIEATRDI GTQMLAGADP AMVFRLIAEE
     ALTLMAGAAT LVAVPLDDEA PACEVDDLVI VEVAGEISPA VKQMTVAVSG TSIGGVFHDR
     TPRRFDRLDL AVDGPVEPGP ALVLPLRAAD TVAGVLVALR SADEQPFSDK QLDMMAAFAD
     QAALAWRLAT AQRQMREVEI LTDRDRIARD LHDHVIQRLF AVGLTLQGAA PRARVPAVRE
     SIYSSIDDLQ EIIQEIRSAI FDLHAGPSRA TGLRHRLDKV IDQLAIPALH TTVQYTGPLS
     VVDTVLANHA EAVLREAVSN AVRHANATSL AINVSVEDDV RVEVVDDGVG ISGDITESGL
     RNLRQRADDA GGEFTVENMP TGGTLLRWSA PLR