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Redox sensor histidine kinase response regulator DevS (EC 2.7.13.3)

 DEVS_MYCTU              Reviewed;         578 AA.
P9WGK3; L0TBM4; P95194; Q79CX7; Q7D626;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 31.
RecName: Full=Oxygen sensor histidine kinase response regulator DevS/DosS {ECO:0000303|PubMed:28977726};
EC=2.7.13.3 {ECO:0000269|PubMed:15033981};
Name=devS {ECO:0000303|PubMed:10970762}; Synonyms=dosS;
OrderedLocusNames=Rv3132c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116, AND OPERON STRUCTURE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10970762; DOI=10.1054/tuld.2000.0240;
Dasgupta N., Kapur V., Singh K.K., Das T.K., Sachdeva S.,
Jyothisri K., Tyagi J.S.;
"Characterization of a two-component system, devR-devS, of
Mycobacterium tuberculosis.";
Tuber. Lung Dis. 80:141-159(2000).
[3]
FUNCTION, REGULON, INDUCTION BY HYPOXIA, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11416222; DOI=10.1073/pnas.121172498;
Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
Schoolnik G.K.;
"Regulation of the Mycobacterium tuberculosis hypoxic response gene
encoding alpha -crystallin.";
Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
[4]
FUNCTION, INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY
REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12953092; DOI=10.1084/jem.20030205;
Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I.,
Dolganov G.M., Sherman D.R., Schoolnik G.K.;
"Inhibition of respiration by nitric oxide induces a Mycobacterium
tuberculosis dormancy program.";
J. Exp. Med. 198:705-713(2003).
[5]
FUNCTION, CATALYTIC ACTIVITY, REGULON, PHOSPHORYLATION AT HIS-395,
AUTOPHOSPHORYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
395-HIS--HIS-397.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15033981; DOI=10.1074/jbc.M401230200;
Roberts D.M., Liao R.P., Wisedchaisri G., Hol W.G., Sherman D.R.;
"Two sensor kinases contribute to the hypoxic response of
Mycobacterium tuberculosis.";
J. Biol. Chem. 279:23082-23087(2004).
[6]
FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT HIS-395,
AUTOPHOSPHORYLATION, COFACTOR, AND MUTAGENESIS OF HIS-395; HIS-397 AND
ASN-503.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15073296; DOI=10.1099/mic.0.26218-0;
Saini D.K., Malhotra V., Dey D., Pant N., Das T.K., Tyagi J.S.;
"DevR-DevS is a bona fide two-component system of Mycobacterium
tuberculosis that is hypoxia-responsive in the absence of the DNA-
binding domain of DevR.";
Microbiology 150:865-875(2004).
[7]
HEME COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-139 AND
HIS-149.
PubMed=16213520; DOI=10.1016/j.jmb.2005.09.011;
Sardiwal S., Kendall S.L., Movahedzadeh F., Rison S.C., Stoker N.G.,
Djordjevic S.;
"A GAF domain in the hypoxia/NO-inducible Mycobacterium tuberculosis
DosS protein binds haem.";
J. Mol. Biol. 353:929-936(2005).
[8]
FUNCTION AS AN OXYGEN SENSOR, HEME COFACTOR, BINDING OF CN; N(3); CO;
O(2) AND NO, AND MUTAGENESIS OF HIS-149.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17371046; DOI=10.1021/bi602422p;
Ioanoviciu A., Yukl E.T., Moenne-Loccoz P., de Montellano P.R.;
"DevS, a heme-containing two-component oxygen sensor of Mycobacterium
tuberculosis.";
Biochemistry 46:4250-4260(2007).
[9]
FUNCTION AS A REDOX SENSOR, LIGAND-BINDING, AND HEME COFACTOR.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17609369; DOI=10.1073/pnas.0705054104;
Kumar A., Toledo J.C., Patel R.P., Lancaster J.R. Jr., Steyn A.J.;
"Mycobacterium tuberculosis DosS is a redox sensor and DosT is a
hypoxia sensor.";
Proc. Natl. Acad. Sci. U.S.A. 104:11568-11573(2007).
[10]
FUNCTION AS AN OXYGEN SENSOR, HEME COFACTOR, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
LIGAND-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17600145; DOI=10.1110/ps.072897707;
Sousa E.H., Tuckerman J.R., Gonzalez G., Gilles-Gonzalez M.A.;
"DosT and DevS are oxygen-switched kinases in Mycobacterium
tuberculosis.";
Protein Sci. 16:1708-1719(2007).
[11]
FUNCTION, MUTAGENESIS OF TYR-171, AND LIGAND-BINDING.
PubMed=18975917; DOI=10.1021/bi801234w;
Yukl E.T., Ioanoviciu A., Nakano M.M., de Montellano P.R.,
Moenne-Loccoz P.;
"A distal tyrosine residue is required for ligand discrimination in
DevS from Mycobacterium tuberculosis.";
Biochemistry 47:12532-12539(2008).
[12]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[13]
FUNCTION IN CARBON MONOXIDE (CO) RESPONSE, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
Shiloh M.U., Manzanillo P., Cox J.S.;
"Mycobacterium tuberculosis senses host-derived carbon monoxide during
macrophage infection.";
Cell Host Microbe 3:323-330(2008).
[14]
INDUCTION BY CARBON MONOXIDE (CO), DISRUPTION PHENOTYPE, AND ROLE IN
DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18400743; DOI=10.1074/jbc.M802274200;
Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S.,
Kramnik I., Agarwal A., Steyn A.J.;
"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
tuberculosis dormancy regulon.";
J. Biol. Chem. 283:18032-18039(2008).
[15]
FUNCTION, HEME COFACTOR, DOMAIN, AND MUTAGENESIS OF TYR-171.
PubMed=19463006; DOI=10.1021/bi802309y;
Ioanoviciu A., Meharenna Y.T., Poulos T.L., Ortiz de Montellano P.R.;
"DevS oxy complex stability identifies this heme protein as a gas
sensor in Mycobacterium tuberculosis dormancy.";
Biochemistry 48:5839-5848(2009).
[16]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=19487478; DOI=10.1128/IAI.01449-08;
Honaker R.W., Leistikow R.L., Bartek I.L., Voskuil M.I.;
"Unique roles of DosT and DosS in DosR regulon induction and
Mycobacterium tuberculosis dormancy.";
Infect. Immun. 77:3258-3263(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[18]
FUNCTION, MUTAGENESIS OF GLU-87; HIS-89 AND ARG-204, AND
LIGAND-BINDING.
STRAIN=H37Rv;
PubMed=27235395; DOI=10.1074/jbc.M116.724815;
Basudhar D., Madrona Y., Yukl E.T., Sivaramakrishnan S., Nishida C.R.,
Moenne-Loccoz P., Ortiz de Montellano P.R.;
"Distal hydrogen-bonding interactions in ligand sensing and signaling
by Mycobacterium tuberculosis DosS.";
J. Biol. Chem. 291:16100-16111(2016).
[19]
FUNCTION.
STRAIN=H37Rv;
PubMed=28977726; DOI=10.1111/febs.14284;
Sousa E.H.S., Gonzalez G., Gilles-Gonzalez M.A.;
"Target DNA stabilizes Mycobacterium tuberculosis DevR/DosR
phosphorylation by the full-length oxygen sensors DevS/DosS and
DosT.";
FEBS J. 284:3954-3967(2017).
[20]
REVIEW.
PubMed=25002970; DOI=10.3390/bios3030259;
Sivaramakrishnan S., de Montellano P.R.;
"The DosS-DosT/DosR mycobacterial sensor system.";
Biosensors 3:259-282(2013).
[21] {ECO:0000244|PDB:2W3D, ECO:0000244|PDB:2W3E, ECO:0000244|PDB:2W3F, ECO:0000244|PDB:2W3G, ECO:0000244|PDB:2W3H}
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 63-210 IN HEME-BOUND;
REDUCED; OXIDIZED AND CYANIDE-BOUND FORMS, AND REDUCTION BY FLAVIN
NUCLEOTIDES.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19276084; DOI=10.1074/jbc.M808905200;
Cho H.Y., Cho H.J., Kim Y.M., Oh J.I., Kang B.S.;
"Structural insight into the heme-based redox sensing by DosS from
Mycobacterium tuberculosis.";
J. Biol. Chem. 284:13057-13067(2009).
[22] {ECO:0000244|PDB:2Y79, ECO:0000244|PDB:2Y8H}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 63-210 IN COMPLEX WITH HEME.
STRAIN=H37Rv;
PubMed=21536032; DOI=10.1016/J.FEBSLET.2011.04.050;
Cho H.Y., Cho H.J., Kim M.H., Kang B.S.;
"Blockage of the channel to heme by the E87 side chain in the GAF
domain of Mycobacterium tuberculosis DosS confers the unique
sensitivity of DosS to oxygen.";
FEBS Lett. 585:1873-1878(2011).
[23] {ECO:0000244|PDB:3ZXO}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 454-578 IN COMPLEX WITH
ZINC, SUBUNIT, DOMAIN, MUTAGENESIS OF HIS-395; ARG-440; CYS-524 AND
GLU-537, AND ATP-BINDING.
STRAIN=H37Rv;
PubMed=23486471; DOI=10.1074/JBC.M112.442467;
Cho H.Y., Lee Y.H., Bae Y.S., Kim E., Kang B.S.;
"Activation of ATP binding for the autophosphorylation of DosS, a
Mycobacterium tuberculosis histidine kinase lacking an ATP lid
motif.";
J. Biol. Chem. 288:12437-12447(2013).
[24] {ECO:0000244|PDB:4YNR, ECO:0000244|PDB:4YOF}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 63-210 IN COMPLEX WITH HEME
AND CO OR NO.
PubMed=27729224; DOI=10.1016/j.abb.2016.10.005;
Madrona Y., Waddling C.A., Ortiz de Montellano P.R.;
"Crystal structures of the CO- and NO-bound DosS GAF-A domain and
implications for DosS signaling in Mycobacterium tuberculosis.";
Arch. Biochem. Biophys. 612:1-8(2016).
-!- FUNCTION: Member of the two-component regulatory system DevR/DevS
(DosR/DosS) involved in onset of the dormancy response
(PubMed:12953092). Regulates an approximately 48-member regulon
(PubMed:12953092, PubMed:11416222, PubMed:15033981,
PubMed:18400743). Required for full induction of the DevR (DosR)
regulon; acts later than DosT to positively regulate expression of
the DevR regulon during adaptation to anaerobiosis
(PubMed:19487478). Characterized as an oxygen sensor; O(2) acts as
a switch, with O(2)-bound Fe(2+) protein inactive in
autophosphorylation (PubMed:17371046, PubMed:17600145,
PubMed:18975917, PubMed:19463006, PubMed:28977726). Has also been
suggested to act as a redox sensor, or perhaps as a dual
oxygen/redox sensor (PubMed:17609369). Autophosphorylates under
anaerobic but not aerobic conditions, binding of NO or CO does not
dramatically change the level of autophosphorylation of Fe(2+)
protein, binding of O(2) inactivates kinase activity
(PubMed:17600145, PubMed:18975917, PubMed:27235395). Binds O(2),
NO, CO (PubMed:17371046, PubMed:17609369, PubMed:17600145,
PubMed:18975917, PubMed:27235395). It is probably reduced by
flavin nucleotides such as FMN and FAD (PubMed:19276084). May be
the primary sensor for CO (PubMed:18400743). Donates a phosphate
group to transcriptional regulator DevR (DosR) (PubMed:15033981,
PubMed:15073296, PubMed:28977726). {ECO:0000269|PubMed:11416222,
ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:15033981,
ECO:0000269|PubMed:15073296, ECO:0000269|PubMed:17371046,
ECO:0000269|PubMed:17600145, ECO:0000269|PubMed:17609369,
ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359,
ECO:0000269|PubMed:18975917, ECO:0000269|PubMed:19463006,
ECO:0000269|PubMed:19487478, ECO:0000269|PubMed:27235395,
ECO:0000269|PubMed:28977726}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine. {ECO:0000269|PubMed:15033981}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15073296,
ECO:0000269|PubMed:17600145};
Note=Mn(2+) will also substitute in autophosphorylation assays,
while Ca(2+) is a poor substitute (PubMed:17600145).
{ECO:0000269|PubMed:17600145};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:16213520,
ECO:0000269|PubMed:17371046, ECO:0000269|PubMed:17600145,
ECO:0000269|PubMed:19463006, ECO:0000269|PubMed:21536032,
ECO:0000269|PubMed:27729224};
Note=Binds 1 heme group per monomer (PubMed:16213520,
PubMed:17371046, PubMed:17600145, PubMed:21536032,
PubMed:27729224). {ECO:0000269|PubMed:16213520,
ECO:0000269|PubMed:17371046, ECO:0000269|PubMed:17600145,
ECO:0000269|PubMed:21536032, ECO:0000269|PubMed:27729224};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=73 uM for ATP for autophosphorylation by deoxy-DevS
{ECO:0000269|PubMed:17600145};
-!- SUBUNIT: The isolated histidine kinase core (HKC, residues 386-
578) is a dimer and autophosphorylates, suggesting the protein may
function as a homodimer (PubMed:23486471).
{ECO:0000269|PubMed:23486471}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16213520,
ECO:0000305|PubMed:17600145}.
-!- INDUCTION: A member of the dormancy regulon, expression is
controlled by devR (PubMed:12953092, PubMed:19487478). Induced in
response to reduced oxygen tension (hypoxia) (PubMed:11416222,
PubMed:12953092, PubMed:19487478). Induced in response to low
levels of nitric oxide (NO) and carbon monoxide (CO)
(PubMed:12953092, PubMed:18400743). It is hoped that this regulon
will give insight into the latent, or dormant phase of infection.
Member of the Rv3134c-devR-devS operon (PubMed:10970762).
{ECO:0000269|PubMed:10970762, ECO:0000269|PubMed:11416222,
ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:19487478}.
-!- DOMAIN: The first GAF domain protects the heme moiety from auto-
oxidation, contributing to the full-length protein's very long
half-life (more than 36 hours in buffers without transition
metals) (PubMed:19463006). The isolated ATP-binding subdomain
(residues 454-578) crystallized in a closed form that is unable to
bind ATP, suggesting that ATP-binding requires conformational
changes in this loop region; in this closed conformation it binds
a zinc atom (PubMed:23486471). The isolated histidine kinase core
(HKC, residues 386-578) both autophosphorylates and phosphorylates
the isolated histidine acceptor subdomain (residues 386-452)
(PubMed:23486471). The relative arrangements of the 2 subdomains
of the HKC may control not only kinase activity but exposure of
the ATP binding site (PubMed:23486471).
{ECO:0000269|PubMed:19463006, ECO:0000269|PubMed:23486471}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show no changes in
gene induction following hypoxia, or exposure to NO or CO
(PubMed:11416222, PubMed:15033981, PubMed:18474359). Another
publication shows a severely attenuated response to CO
(PubMed:18400743). Cells lacking both this gene and DosT have no
response to hypoxia, or exposure to NO or CO showing both proteins
are required for the hypoxic, NO and CO responses
(PubMed:15033981). 95% decreased induction of the DevR (DosR)
regulon during anaerobic growth, 50% decreased induction of the
DevR regulon upon exposure to NO during aerobic growth
(PubMed:19487478). {ECO:0000269|PubMed:11416222,
ECO:0000269|PubMed:15033981, ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:18474359, ECO:0000269|PubMed:19487478}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
{ECO:0000305|PubMed:19099550}.
-!- MISCELLANEOUS: A tyrosine residue (Tyr-171) is required for
discrimination between bound gaseous ligands (PubMed:18975917).
The Tyr is part of a probable hydrogen bonding network which
includes Glu-87, His-89 and Arg-204 that is probably also
important for signaling to the kinase domain (PubMed:19276084,
PubMed:27235395). {ECO:0000269|PubMed:18975917,
ECO:0000305|PubMed:19276084, ECO:0000305|PubMed:27235395}.
-!- MISCELLANEOUS: The dev nomenclature derives from the increased
expression (differentially expressed in virulent strain, dev) of
these genes in virulent H37Rv versus avirulent H37Ra. The dos
nomenclature derives from experiments in M.bovis showing the same
genes are essential for dormancy survival.
{ECO:0000305|PubMed:25002970}.
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EMBL; AL123456; CCP45942.1; -; Genomic_DNA.
EMBL; U22037; AAD17453.1; -; Genomic_DNA.
PIR; E70645; E70645.
RefSeq; NP_217648.1; NC_000962.3.
RefSeq; WP_003899933.1; NZ_KK339370.1.
PDB; 2W3D; X-ray; 2.00 A; A/B=63-210.
PDB; 2W3E; X-ray; 1.60 A; A/B=63-210.
PDB; 2W3F; X-ray; 1.60 A; A/B=63-210.
PDB; 2W3G; X-ray; 1.40 A; A/B=63-210.
PDB; 2W3H; X-ray; 1.80 A; A/B=63-210.
PDB; 2Y79; X-ray; 1.80 A; A/B=63-210.
PDB; 2Y8H; X-ray; 1.90 A; A/B=63-210.
PDB; 3ZXO; X-ray; 1.90 A; A/B=454-578.
PDB; 4YNR; X-ray; 1.92 A; A/B=63-210.
PDB; 4YOF; X-ray; 1.90 A; A/B=63-210.
PDBsum; 2W3D; -.
PDBsum; 2W3E; -.
PDBsum; 2W3F; -.
PDBsum; 2W3G; -.
PDBsum; 2W3H; -.
PDBsum; 2Y79; -.
PDBsum; 2Y8H; -.
PDBsum; 3ZXO; -.
PDBsum; 4YNR; -.
PDBsum; 4YOF; -.
ProteinModelPortal; P9WGK3; -.
SMR; P9WGK3; -.
IntAct; P9WGK3; 1.
STRING; 83332.Rv3132c; -.
iPTMnet; P9WGK3; -.
PaxDb; P9WGK3; -.
EnsemblBacteria; CCP45942; CCP45942; Rv3132c.
GeneID; 888829; -.
KEGG; mtu:Rv3132c; -.
TubercuList; Rv3132c; -.
eggNOG; ENOG4107EFD; Bacteria.
eggNOG; COG2203; LUCA.
eggNOG; COG4585; LUCA.
KO; K07682; -.
OMA; NCKKHAG; -.
PhylomeDB; P9WGK3; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
GO; GO:0070025; F:carbon monoxide binding; IDA:MTBBASE.
GO; GO:0020037; F:heme binding; IDA:MTBBASE.
GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
GO; GO:0070026; F:nitric oxide binding; IDA:MTBBASE.
GO; GO:0019825; F:oxygen binding; IDA:MTBBASE.
GO; GO:0019826; F:oxygen sensor activity; IDA:MTBBASE.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
GO; GO:0070483; P:detection of hypoxia; IEA:InterPro.
GO; GO:0051776; P:detection of redox state; IDA:MTBBASE.
GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
GO; GO:0051775; P:response to redox state; IDA:MTBBASE.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.450.40; -; 2.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR027035; DosT/DevS.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
PANTHER; PTHR43336; PTHR43336; 1.
Pfam; PF13185; GAF_2; 2.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF07730; HisKA_3; 1.
SMART; SM00065; GAF; 2.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS50109; HIS_KIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Heme; Iron; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Transferase;
Two-component regulatory system.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609}.
CHAIN 2 578 Oxygen sensor histidine kinase response
regulator DevS/DosS.
/FTId=PRO_0000392623.
DOMAIN 63 200 GAF 1.
DOMAIN 231 369 GAF 2.
DOMAIN 383 578 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
REGION 386 452 Histidine acceptor domain.
{ECO:0000305|PubMed:23486471}.
REGION 454 578 ATP-binding domain.
{ECO:0000305|PubMed:23486471}.
METAL 149 149 Iron (heme axial ligand); via tele
nitrogen. {ECO:0000269|PubMed:19276084,
ECO:0000269|PubMed:21536032,
ECO:0000269|PubMed:27729224}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:21969609}.
MOD_RES 395 395 Phosphohistidine; by autocatalysis.
{ECO:0000305|PubMed:15033981,
ECO:0000305|PubMed:15073296}.
MUTAGEN 87 87 E->A: No change in autophosphorylation
when NO-bound, decreased
autophosphorylation in deoxy or CO-bound
state, slightly increased activity in
O(2)-bound state.
{ECO:0000269|PubMed:27235395}.
MUTAGEN 87 87 E->D: No change in autophosphorylation
when NO-bound, loss of
autophosphorylation in deoxy or CO-bound
state. {ECO:0000269|PubMed:27235395}.
MUTAGEN 87 87 E->G: No change in autophosphorylation
when deoxy or NO-bound, decreased
autophosphorylation when CO-bound,
increased activity in O(2)-bound state.
{ECO:0000269|PubMed:27235395}.
MUTAGEN 89 89 H->A: No autophosphorylation activity no
matter the bound gaseous ligand, protein
more easily oxidized to Fe(3+) state.
{ECO:0000269|PubMed:27235395}.
MUTAGEN 89 89 H->R: Decreased autophosphorylation when
CO- or NO-bound, none in the deoxy or
O(2)-bound state, protein more easily
oxidized to Fe(3+) state.
{ECO:0000269|PubMed:27235395}.
MUTAGEN 139 139 H->A: No change in heme binding.
{ECO:0000269|PubMed:16213520}.
MUTAGEN 149 149 H->A: Weaker than wild-type heme binding.
{ECO:0000269|PubMed:16213520,
ECO:0000269|PubMed:17371046}.
MUTAGEN 171 171 Y->F: No autophosphorylation when Fe(2+)
protein is bound to CO or NO; no change
in autophosphorylation of deoxy-protein.
No change in auto-oxidation, slightly
higher affinity for O(2) and CO.
{ECO:0000269|PubMed:18975917,
ECO:0000269|PubMed:19463006}.
MUTAGEN 204 204 R->A: No autophosphorylation activity no
matter the bound gaseous ligand.
{ECO:0000269|PubMed:27235395}.
MUTAGEN 395 397 HDH->KDK: No autophosphorylation, no
transfer to DevR (DosR).
{ECO:0000269|PubMed:15033981}.
MUTAGEN 395 395 H->Q: No autophosphorylation. Isolated
kinase core binds ATP.
{ECO:0000269|PubMed:15073296,
ECO:0000269|PubMed:23486471}.
MUTAGEN 397 397 H->A,Q: No change in phosphorylation.
{ECO:0000269|PubMed:15073296}.
MUTAGEN 440 440 R->C: Can form a disulfide bond; when
associated with C-537. Loss of
autophosphorylation; when associated with
C-524 or C-524 and C-537.
{ECO:0000269|PubMed:23486471}.
MUTAGEN 503 503 N->D: No autophosphorylation.
{ECO:0000269|PubMed:15073296}.
MUTAGEN 524 524 C->S: Isolated kinase core no longer
forms dimers, autophosphorylation
unaffected. Decreased
autophosphorylation; when associated with
C-537. Loss of autophosphorylation; when
associated with C-440 or C-440 and C-537.
{ECO:0000269|PubMed:23486471}.
MUTAGEN 537 537 E->C: Can form a disulfide bond; when
associated with C-440. Decreased
autophosphorylation; when associated with
C-524. Loss of autophosphorylation; when
associated with C-440 or C-440 and C-524.
{ECO:0000269|PubMed:23486471}.
HELIX 63 78 {ECO:0000244|PDB:2W3G}.
STRAND 81 89 {ECO:0000244|PDB:2W3G}.
HELIX 91 93 {ECO:0000244|PDB:2W3E}.
STRAND 95 102 {ECO:0000244|PDB:2W3G}.
HELIX 105 111 {ECO:0000244|PDB:2W3G}.
HELIX 120 126 {ECO:0000244|PDB:2W3G}.
STRAND 131 135 {ECO:0000244|PDB:2W3G}.
HELIX 136 138 {ECO:0000244|PDB:2W3G}.
STRAND 155 162 {ECO:0000244|PDB:2W3G}.
STRAND 165 175 {ECO:0000244|PDB:2W3G}.
HELIX 183 206 {ECO:0000244|PDB:2W3G}.
HELIX 456 467 {ECO:0000244|PDB:3ZXO}.
STRAND 472 480 {ECO:0000244|PDB:3ZXO}.
HELIX 482 484 {ECO:0000244|PDB:3ZXO}.
HELIX 487 503 {ECO:0000244|PDB:3ZXO}.
STRAND 512 529 {ECO:0000244|PDB:3ZXO}.
TURN 535 538 {ECO:0000244|PDB:3ZXO}.
HELIX 541 552 {ECO:0000244|PDB:3ZXO}.
STRAND 556 561 {ECO:0000244|PDB:3ZXO}.
TURN 563 565 {ECO:0000244|PDB:3ZXO}.
STRAND 568 576 {ECO:0000244|PDB:3ZXO}.
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


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