KDPD_ECOLI
ID KDPD_ECOLI Reviewed; 894 AA.
AC P21865;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Sensor protein KdpD;
DE EC=2.7.13.3;
GN Name=kdpD; OrderedLocusNames=b0695, JW0683;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=1532388; DOI=10.1128/jb.174.7.2152-2159.1992;
RA Walderhaug M.O., Polarek J.W., Voelkner P., Daniel J.M., Hesse J.E.,
RA Altendorf K., Epstein W.;
RT "KdpD and KdpE, proteins that control expression of the kdpABC operon, are
RT members of the two-component sensor-effector class of regulators.";
RL J. Bacteriol. 174:2152-2159(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY.
RX PubMed=7499326; DOI=10.1074/jbc.270.47.28282;
RA Zimmann P., Puppe W., Altendorf K.;
RT "Membrane topology analysis of the sensor kinase KdpD of Escherichia
RT coli.";
RL J. Biol. Chem. 270:28282-28288(1995).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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. {ECO:0000269|PubMed:1532388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- INTERACTION:
CC P21865; P21866: kdpE; NbExp=5; IntAct=EBI-1123100, EBI-6403634;
CC P21865; P69829: ptsN; NbExp=4; IntAct=EBI-1123100, EBI-547017;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1532388};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1532388}.
CC -!- SIMILARITY: In the central section; belongs to the universal stress
CC protein A family. {ECO:0000305}.
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DR EMBL; M36066; AAA24041.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73789.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35352.1; -; Genomic_DNA.
DR PIR; B42372; B42372.
DR RefSeq; NP_415223.1; NC_000913.3.
DR RefSeq; WP_001310640.1; NZ_SSZK01000045.1.
DR PDB; 2KSF; NMR; -; A=397-502.
DR PDB; 4QPR; X-ray; 1.55 A; A=515-646.
DR PDB; 4Y2F; X-ray; 1.40 A; A=515-646.
DR PDB; 6LGQ; X-ray; 3.00 A; C=661-894.
DR PDBsum; 2KSF; -.
DR PDBsum; 4QPR; -.
DR PDBsum; 4Y2F; -.
DR PDBsum; 6LGQ; -.
DR AlphaFoldDB; P21865; -.
DR BMRB; P21865; -.
DR SMR; P21865; -.
DR BioGRID; 4259925; 12.
DR BioGRID; 851085; 3.
DR DIP; DIP-10062N; -.
DR IntAct; P21865; 6.
DR STRING; 511145.b0695; -.
DR jPOST; P21865; -.
DR PaxDb; P21865; -.
DR PRIDE; P21865; -.
DR EnsemblBacteria; AAC73789; AAC73789; b0695.
DR EnsemblBacteria; BAA35352; BAA35352; BAA35352.
DR GeneID; 946744; -.
DR KEGG; ecj:JW0683; -.
DR KEGG; eco:b0695; -.
DR PATRIC; fig|1411691.4.peg.1580; -.
DR EchoBASE; EB0511; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_0_6; -.
DR InParanoid; P21865; -.
DR OMA; LWATAFQ; -.
DR PhylomeDB; P21865; -.
DR BioCyc; EcoCyc:KDPD-MON; -.
DR BioCyc; MetaCyc:KDPD-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P21865; -.
DR PRO; PR:P21865; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IDA:EcoCyc.
DR GO; GO:0035865; P:cellular response to potassium ion; IDA:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IMP:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.20.120.620; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..894
FT /note="Sensor protein KdpD"
FT /id="PRO_0000074772"
FT TOPO_DOM 1..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 424..427
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 428..444
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 467..474
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 475..498
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 499..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 670..883
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 673
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:2KSF"
FT HELIX 402..420
FT /evidence="ECO:0007829|PDB:2KSF"
FT HELIX 430..443
FT /evidence="ECO:0007829|PDB:2KSF"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:2KSF"
FT HELIX 475..498
FT /evidence="ECO:0007829|PDB:2KSF"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:4Y2F"
FT HELIX 528..543
FT /evidence="ECO:0007829|PDB:4Y2F"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:4Y2F"
FT HELIX 572..581
FT /evidence="ECO:0007829|PDB:4Y2F"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:4Y2F"
FT STRAND 595..604
FT /evidence="ECO:0007829|PDB:4Y2F"
FT STRAND 607..617
FT /evidence="ECO:0007829|PDB:4Y2F"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:4Y2F"
FT HELIX 625..646
FT /evidence="ECO:0007829|PDB:4Y2F"
FT HELIX 662..674
FT /evidence="ECO:0007829|PDB:6LGQ"
FT HELIX 676..695
FT /evidence="ECO:0007829|PDB:6LGQ"
FT HELIX 701..726
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:6LGQ"
FT HELIX 741..752
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 770..773
FT /evidence="ECO:0007829|PDB:6LGQ"
FT HELIX 775..792
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 799..816
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:6LGQ"
FT HELIX 849..858
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 862..867
FT /evidence="ECO:0007829|PDB:6LGQ"
FT STRAND 869..880
FT /evidence="ECO:0007829|PDB:6LGQ"
SQ SEQUENCE 894 AA; 98718 MW; E9D2749B4CAA12DA CRC64;
MNNEPLRPDP DRLLEQTAAP HRGKLKVFFG ACAGVGKTWA MLAEAQRLRA QGLDIVVGVV
ETHGRKDTAA MLEGLAVLPL KRQAYRGRHI SEFDLDAALA RRPALILMDE LAHSNAPGSR
HPKRWQDIEE LLEAGIDVFT TVNVQHLESL NDVVSGVTGI QVRETVPDPF FDAADDVVLV
DLPPDDLRQR LKEGKVYIAG QAERAIEHFF RKGNLIALRE LALRRTADRV DEQMRAWRGH
PGEEKVWHTR DAILLCIGHN TGSEKLVRAA ARLASRLGSV WHAVYVETPA LHRLPEKKRR
AILSALRLAQ ELGAETATLS DPAEEKAVVR YAREHNLGKI ILGRPASRRW WRRETFADRL
ARIAPDLDQV LVALDEPPAR TINNAPDNRS FKDKWRVQIQ GCVVAAALCA VITLIAMQWL
MAFDAANLVM LYLLGVVVVA LFYGRWPSVV ATVINVVSFD LFFIAPRGTL AVSDVQYLLT
FAVMLTVGLV IGNLTAGVRY QARVARYREQ RTRHLYEMSK ALAVGRSPQD IAATSEQFIA
STFHARSQVL LPDDNGKLQP LTHPQGMTPW DDAIAQWSFD KGLPAGAGTD TLPGVPYQIL
PLKSGEKTYG LVVVEPGNLR QLMIPEQQRL LETFTLLVAN ALERLTLTAS EEQARMASER
EQIRNALLAA LSHDLRTPLT VLFGQAEILT LDLASEGSPH ARQASEIRQH VLNTTRLVNN
LLDMARIQSG GFNLKKEWLT LEEVVGSALQ MLEPGLSSPI NLSLPEPLTL IHVDGPLFER
VLINLLENAV KYAGAQAEIG IDAHVEGENL QLDVWDNGPG LPPGQEQTIF DKFARGNKES
AVPGVGLGLA ICRAIVDVHG GTITAFNRPE GGACFRVTLP QQTAPELEEF HEDM
