KDPD_MYCTU
ID KDPD_MYCTU Reviewed; 860 AA.
AC P9WGL3; L0T881; P96372;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Sensor protein KdpD;
DE EC=2.7.13.3 {ECO:0000269|PubMed:24667597};
GN Name=kdpD; OrderedLocusNames=Rv1028c; ORFNames=MTCY10G2.21;
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12595424; DOI=10.1128/iai.71.3.1134-1140.2003;
RA Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J., Stoker N.G.;
RT "Deletion of two-component regulatory systems increases the virulence of
RT Mycobacterium tuberculosis.";
RL Infect. Immun. 71:1134-1140(2003).
RN [3]
RP POSSIBLE INTERACTION WITH LPRF AND LPRJ, INDUCTION, TOPOLOGY, AND
RP EXPRESSION IN M.SMEGMATIS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12581360; DOI=10.1046/j.1365-2958.2003.03356.x;
RA Steyn A.J., Joseph J., Bloom B.R.;
RT "Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD
RT with members of the Lpr family.";
RL Mol. Microbiol. 47:1075-1089(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT
RP HIS-642, MUTAGENESIS OF HIS-642, AND COFACTOR.
RX PubMed=24667597; DOI=10.1016/j.bbrc.2014.03.066;
RA Agrawal R., Saini D.K.;
RT "Rv1027c-Rv1028c encode functional KdpDE two--component system in
RT Mycobacterium tuberculosis.";
RL Biochem. Biophys. Res. Commun. 446:1172-1178(2014).
CC -!- FUNCTION: Member of the two-component regulatory system KdpD/KdpE
CC involved in the regulation of the kdp operon. Functions as a sensor
CC protein kinase which is autophosphorylated at a histidine residue and
CC transfers its phosphate group to the conserved aspartic acid residue in
CC the regulatory domain of KdpE in response to environmental signals such
CC as low levels of potassium ion, osmotic imbalance, acid and nutrient
CC stresses. In turn, KdpE binds to the upstream promoter regions of
CC target genes to positively regulate their expression.
CC {ECO:0000269|PubMed:24667597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:24667597};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24667597};
CC -!- SUBUNIT: May interact with lipoproteins LprF and LprJ.
CC {ECO:0000305|PubMed:12581360}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12581360};
CC Multi-pass membrane protein {ECO:0000305|PubMed:12581360}.
CC -!- INDUCTION: Induced at low K(+) concentrations (in M.tuberculosis);
CC overexpression of LprF or LprJ increases expression of this gene at 0
CC and 250 uM K(+) (in M.smegmatis). {ECO:0000269|PubMed:12581360}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:24667597}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking KdpD and KdpE show an increase in
CC virulence in mouse model of infection, with significantly shorter
CC survival times. {ECO:0000269|PubMed:12595424}.
CC -!- SIMILARITY: In the central section; belongs to the universal stress
CC protein A family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43778.1; -; Genomic_DNA.
DR PIR; G70623; G70623.
DR RefSeq; NP_215544.1; NC_000962.3.
DR RefSeq; WP_003915886.1; NZ_NVQJ01000018.1.
DR AlphaFoldDB; P9WGL3; -.
DR SMR; P9WGL3; -.
DR IntAct; P9WGL3; 1.
DR STRING; 83332.Rv1028c; -.
DR PaxDb; P9WGL3; -.
DR GeneID; 886084; -.
DR KEGG; mtu:Rv1028c; -.
DR TubercuList; Rv1028c; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; LWATAFQ; -.
DR PhylomeDB; P9WGL3; -.
DR BRENDA; 2.7.13.3; 3445.
DR PHI-base; PHI:3618; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.20.120.620; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..860
FT /note="Sensor protein KdpD"
FT /id="PRO_0000074773"
FT TOPO_DOM 1..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12581360"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..428
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12581360"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..510
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..860
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12581360"
FT DOMAIN 639..857
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 642
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:24667597"
FT MUTAGEN 642
FT /note="H->Q: Complete loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:24667597"
SQ SEQUENCE 860 AA; 92749 MW; 0494DA140A6B04C2 CRC64;
MTLLFADLCA IFTPYRWMIE HVTTKRGQLR IYLGAAPGVG KTYAMLGEAH RRLERGTDVV
AAVVETHGRN KTAKLLEGIE MIPPRYVEYR GARFPELDVE AVLRRHPQVV LVDELAHTNT
PGSKNPKRWQ DVQEILDAGI TVISTVNIQH LEGLNDVVEQ ITGIEQKEKI PDEIVRAADQ
VELVDITPEA LRRRLAHGNV YAAERVDAAL SNYFRTGNLT ALREIALLWL ADQVDAALEK
YRADKKITAT WEARERVVVA VTGGPESETL VRRASRIASK SSAELMVVHV IRGDGLAGVS
APQLGRVREL ATSLGATMHT VVGDDVPTAL LDFAREMNAT QLVVGTSRRS RWARLFDEGI
GARTVQEPGG IDVHMVTHPA ASRASGWSRV SPRERHIASW LAALVVPSVI CAITVAWLDR
FMGIGGESAL FFIGVLIVAL LGGVAPAALS ALLSGMLLNY FLTEPRYTWT IAEPDAAVTE
FVLLAMAVAV AVLVDGAASR TREARRASQE AELLALFAGS VLRGADLATL LQRVRETYSQ
RAVTMLRVRQ GASTGETVAC VGTNPCRDVD SADTAIEVGD DEFWMLMAGR KLAARDRRVL
TAVATQAAGL VKQRELAEEA GQAEAIARAD ELRRSLLSAV SHDLRTPLAA AKVAVSSLRT
EDVAFSPEDT AELLATIEES IDQLTALVAN LLDSSRLAAG VIRPQLRRAY LEEAVQRALV
SIGKGATGFY RSGIDRVKVD VGDAVAMADA GLLERVLANL IDNALRYAPD CVVRVNAGRV
RERVLINVID EGPGVPRGTE EQLFAPFQRP GDHDNTTGVG LGMSVARGFV EAMGGTISAT
DTPGGGLTVV IDLAAPEDRP
