KDPD_MYCTO
ID KDPD_MYCTO Reviewed; 860 AA.
AC P9WGL2; L0T881; P96372;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Sensor protein KdpD;
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P9WGL3};
GN Name=kdpD; OrderedLocusNames=MT1057;
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: 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:0000250|UniProtKB:P9WGL3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P9WGL3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WGL3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P9WGL3}.
CC -!- SIMILARITY: In the central section; belongs to the universal stress
CC protein A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK45309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK45309.1; ALT_INIT; Genomic_DNA.
DR PIR; G70623; G70623.
DR RefSeq; WP_003898694.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGL2; -.
DR SMR; P9WGL2; -.
DR EnsemblBacteria; AAK45309; AAK45309; MT1057.
DR KEGG; mtc:MT1057; -.
DR PATRIC; fig|83331.31.peg.1135; -.
DR HOGENOM; CLU_000445_113_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..860
FT /note="Sensor protein KdpD"
FT /id="PRO_0000428342"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 860 AA; 92739 MW; 3DB0485D2E5F5677 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
GARTVQESGG 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
