ID   DEVS_MYCTO              Reviewed;         578 AA.
AC   P9WGK2; L0TBM4; P95194; Q79CX7; Q7D626;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Oxygen sensor histidine kinase response regulator DevS/DosS {ECO:0000305};
DE            EC=2.7.13.3;
GN   Name=devS; Synonyms=dosS; OrderedLocusNames=MT3218;
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).
RN   [2]
RP   INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12953092; DOI=10.1084/jem.20030205;
RA   Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA   Sherman D.R., Schoolnik G.K.;
RT   "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT   tuberculosis dormancy program.";
RL   J. Exp. Med. 198:705-713(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system DevR/DevS
CC       (DosR/DosS) involved in onset of the dormancy response. Regulates an
CC       approximately 48-member regulon (PubMed:12953092). Required for full
CC       induction of the DevR (DosR) regulon; acts later than DosT to
CC       positively regulate expression of the DevR regulon during adaptation to
CC       anaerobiosis (By similarity). Characterized as an oxygen sensor; O(2)
CC       acts as a switch, with O(2)-bound Fe(2+) protein inactive in
CC       autophosphorylation (By similarity). Has also been suggested to act as
CC       a redox sensor, or perhaps as a dual oxygen/redox sensor (By
CC       similarity). Donates a phosphate group to transcriptional regulator
CC       DevR (DosR) (By similarity). {ECO:0000250|UniProtKB:P9WGK3,
CC       ECO:0000269|PubMed:12953092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WGK3};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P9WGK3};
CC       Note=Binds 1 heme group per monomer. {ECO:0000250|UniProtKB:P9WGK3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WGK3}.
CC   -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC       reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC       {ECO:0000269|PubMed:12953092}.
CC   -!- MISCELLANEOUS: The dev nomenclature derives from the increased
CC       expression (differentially expressed in virulent strain, dev) of these
CC       genes in virulent H37Rv versus avirulent H37Ra. The dos nomenclature
CC       derives from experiments in M.bovis showing the same genes are
CC       essential for dormancy survival. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47556.1; -; Genomic_DNA.
DR   PIR; E70645; E70645.
DR   RefSeq; WP_003899933.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGK2; -.
DR   SMR; P9WGK2; -.
DR   EnsemblBacteria; AAK47556; AAK47556; MT3218.
DR   KEGG; mtc:MT3218; -.
DR   PATRIC; fig|83331.31.peg.3468; -.
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; IPR005467; His_kinase_dom.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   Pfam; PF13185; GAF_2; 2.
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.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Heme; Iron; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW   Repeat; Transferase; Two-component regulatory system.
FT   CHAIN           1..578
FT                   /note="Oxygen sensor histidine kinase response regulator
FT                   DevS/DosS"
FT                   /id="PRO_0000428347"
FT   DOMAIN          63..200
FT                   /note="GAF 1"
FT   DOMAIN          231..369
FT                   /note="GAF 2"
FT   DOMAIN          383..578
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         149
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         395
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   578 AA;  62241 MW;  4C04B836791B9B32 CRC64;
     MTTGGLVDEN DGAAMRPLRH TLSQLRLHEL LVEVQDRVEQ IVEGRDRLDG LVEAMLVVTA
     GLDLEATLRA IVHSATSLVD ARYGAMEVHD RQHRVLHFVY EGIDEETVRR IGHLPKGLGV
     IGLLIEDPKP LRLDDVSAHP ASIGFPPYHP PMRTFLGVPV RVRDESFGTL YLTDKTNGQP
     FSDDDEVLVQ ALAAAAGIAV ANARLYQQAK ARQSWIEATR DIATELLSGT EPATVFRLVA
     AEALKLTAAD AALVAVPVDE DMPAADVGEL LVIETVGSAV ASIVGRTIPV AGAVLREVFV
     NGIPRRVDRV DLEGLDELAD AGPALLLPLR ARGTVAGVVV VLSQGGPGAF TDEQLEMMAA
     FADQAALAWQ LATSQRRMRE LDVLTDRDRI ARDLHDHVIQ RLFAIGLALQ GAVPHERNPE
     VQQRLSDVVD DLQDVIQEIR TTIYDLHGAS QGITRLRQRI DAAVAQFADS GLRTSVQFVG
     PLSVVDSALA DQAEAVVREA VSNAVRHAKA STLTVRVKVD DDLCIEVTDN GRGLPDEFTG
     SGLTNLRQRA EQAGGEFTLA SVPGASGTVL RWSAPLSQ