ID   KDPD_RATRA              Reviewed;         854 AA.
AC   O34971;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Sensor protein KdpD;
DE            EC=2.7.13.3;
GN   Name=kdpD;
OS   Rathayibacter rathayi (Corynebacterium rathayi).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Rathayibacter.
OX   NCBI_TaxID=33887;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2J;
RA   Labadie J.C.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system KdpD/KdpE
CC       involved in the regulation of the kdp operon. KdpD may function as a
CC       membrane-associated protein kinase that phosphorylates KdpE in response
CC       to environmental signals (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {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; AJ002069; CAA05169.1; -; Genomic_DNA.
DR   EMBL; AF030293; AAB84261.1; -; Genomic_DNA.
DR   AlphaFoldDB; O34971; -.
DR   SMR; O34971; -.
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   Gene3D; 1.20.120.620; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 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..854
FT                   /note="Sensor protein KdpD"
FT                   /id="PRO_0000074774"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          625..837
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         628
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   854 AA;  90671 MW;  201867CADFDBB865 CRC64;
     MLVGARVLLG APRGVGKTFT MLEEAKPLRD EGVDVVVAVV ETHGRAGTAA ALVGLEVVPR
     LTVEHRGVVL TEMDVAGVIV RRAPQLALVD ELAHTNASRQ RTEKRWQDVE AILDAGIDVM
     STVNIQHIES LTDVVHKITG APQRETIPDE VLRAAREIEV IDVTPVAAGA LASGLVYPAE
     RIDAALSNYF RLGNLTGLRE LALLWLADEV DSALKNYRAE QGIDSTWETR ERVVVALTGG
     PEGDSHPPGA THCRPCGRGE LLAVHVTGQD GFAPPTRGLW RQRSLVESLG GSYHQVIGDD
     IALVEFARAA NATQLVIGVS RRGRLARRCP VRGSVDGHRE SGNIDVHIVN HAAAGGRFTL
     PRMAGGALTV KRRLSGLALT LILGPLITAV LVTFRSPDSI TSDVLTYQVL VVLVALVGGI
     WPALLAAVLS GITLDYFLVE PLFTVTVDKP LHLFALALYI TIAMMVSYVV DQAARRTRVA
     RRSAAESELL ATIAGSVLRG DGALQSLVSR TRKVWVEGCD CWMPRVRPIT PTRPPGADGQ
     TAADHAVICA DGEPASDDRV VLVPVGERAT LELHGADLDA SERRLLAVIA AQIDAALEHE
     ALSVTAREVG PLAETDRVRT ALLSAVSHDL RRPFDGGNQK GGWLALHRDD PVCRRPGGAA
     RDRRRKPAHL SVLVTDLLDV SRVQAGVLGV TVRQVDVEDV LPRALDELGV GPDQVVLDLD
     AAVGPVLADP GLLQRVLVNL LANALRFSPE GAVPTIDQSF GDTVQIRVTD HGPGIAADRR
     DDVFVPFQRL GDTDNSTGLG LGLALSKGFT VGMGGELDTE DTPGGGLTMV VTLPVASADA
     DANADRPGGS RASL