KDPD_CLOAB
ID KDPD_CLOAB Reviewed; 900 AA.
AC P94608;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Sensor protein KdpD;
DE EC=2.7.13.3;
GN Name=kdpD; OrderedLocusNames=CA_C3678;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=9226259; DOI=10.1128/jb.179.14.4501-4512.1997;
RA Treuner-Lange A., Kuhn A., Duerre P.;
RT "The kdp system of Clostridium acetobutylicum: cloning, sequencing, and
RT transcriptional regulation in response to potassium concentration.";
RL J. Bacteriol. 179:4501-4512(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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 -!- SIMILARITY: In the central section; belongs to the universal stress
CC protein A family. {ECO:0000305}.
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DR EMBL; U39673; AAB39095.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK81599.1; -; Genomic_DNA.
DR PIR; D97351; D97351.
DR RefSeq; NP_350259.1; NC_003030.1.
DR RefSeq; WP_010966939.1; NC_003030.1.
DR AlphaFoldDB; P94608; -.
DR SMR; P94608; -.
DR STRING; 272562.CA_C3678; -.
DR EnsemblBacteria; AAK81599; AAK81599; CA_C3678.
DR GeneID; 45000176; -.
DR KEGG; cac:CA_C3678; -.
DR PATRIC; fig|272562.8.peg.3867; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_1_9; -.
DR OMA; DMPVGDH; -.
DR OrthoDB; 1293707at2; -.
DR BRENDA; 2.7.13.3; 1452.
DR Proteomes; UP000000814; 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; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
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; 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 Pfam; PF13493; DUF4118; 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; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..900
FT /note="Sensor protein KdpD"
FT /id="PRO_0000074771"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 683..900
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 686
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 678
FT /note="S -> R (in Ref. 1; AAB39095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 101360 MW; 74F0A65705ECC070 CRC64;
MDINYERPDP YYLLNKIDKE EKNKNRGKLK IFFGYAAGVG KTYAMLRAAH YMKELGKDIV
IGYIEPHARM DTMSLTKGLP QIPVKNIDYK GVILREFDVD KALLRKPEII LVDELAHTNA
KSQRNKKRWK DIEELLDAGI DVYTTLNVQH IESLNDIVAN ITHVSVRETI PDKVFDDADK
VELIDIEPDE LLKRFTDGKI YRKEQVKRAF NNFFTKNNLY ALREIALRRT ADRVNFEIEI
ARLSKGQITV MATSDQILAC IGTSPSSARI IRTAARMAES YHSKWIALYV DTGRSLGKAD
KETLNANFNL VELLGGELVT VHGENVADQI IRYAELRNTT KIVIGKNHKR TGTLLHFYAK
DVVDKLMDSN SYIDVYMIPN SSYYRDHKNS ILSKISIQHK GSVKDVLKAI IIMAITTDIA
ELFSYMGFKD VNVIMIFILG VIIVYMATKG QIMGIISSIA AVLVFNYRFT EPKNSFIVYD
KSYLVTFPIM MIVAFIIGSL TNKVQKEAQD SNMREKRTQT LYIVSGKLLS AVGTSEVVSI
GIKYISRLVN RNVICYLADT SNKLSTPFVY KKDKGAKEEI IMSKDENAAA YWTFLNGKES
GCGTSTFYRA KGYYIPIKIK NKVLGVIGVS CPSGPLRPQK KAVVDTVTGQ IAIALDREIL
SKEQEKSKVE IERERLRSNL LRSISHDLRS PLAGIKGAAS TILENGELID EKRKQELING
IYEDTEWLIR LIENLLSMTK FDEGNTKIKK DVELVEEVVS EAVQRSSKYF KNHKIKVSVP
EDVIMVSMDG SLIEQVIINL LDNASKFSPK GSTIEIKVYE KKKDVVFEII DEGQGISEDI
LPNIFDRFFT NGSKISDSRR GVGLGLAICK SIVEAHGGKI EAVNKGSGGA IFKFNIPKEL
