ID K9ZY62_DEIPD Unreviewed; 633 AA.
AC K9ZY62;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Deipe_0524 {ECO:0000313|EMBL:AFZ66119.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ66119.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003382; AFZ66119.1; -; Genomic_DNA.
DR AlphaFoldDB; K9ZY62; -.
DR STRING; 937777.Deipe_0524; -.
DR KEGG; dpd:Deipe_0524; -.
DR PATRIC; fig|937777.3.peg.527; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_21_0; -.
DR OrthoDB; 9759607at2; -.
DR Proteomes; UP000010467; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16921; HATPase_FilI-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ66119.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW Transferase {ECO:0000313|EMBL:AFZ66119.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..618
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 352..401
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 633 AA; 70260 MW; 6A0A741303887A46 CRC64;
MPSASGTNWS LAARVTLLFA LLAALIVLGL LSAVWYQAKA QAEDDQRAYL TRLARVAARS
LDTDMSARFE DVAFVAGLAE LRSAPAQEQR QLLERLQRRH PEFAWLGLAD PQGRVRAATG
GLLEGQDVQT QPWFRRGLTG AALGDVHAAE LLAEFLPGAH NEPLRLVDIS VPVLDEDGRL
RGVLGAHLSW SWLARVELSV HELAPAERPV EVLILDRRGR VLHGEAASPV ARPESTPNTG
EAEGREHVTN HVVQARGFLS SLSLAQGQDA YPGLGWQVLV RQQSGTVLVP IAHRQRQVLG
WGAASVALLS LLAWWGARWA TDPLQRLQHS VAGMLDDPAP VGVNEVRGYR EVEQLSASLA
GLAARLRARE EEQKRWRARL EQRLSEEHAQ LQQTNEELET FSYSVSHDLR APLRHVQGFV
GMVRRSMAER LDDKSARYLT VIEGSASRMD ALIDALLDYS RTSRRPMHPV SVDLNMLIEQ
AQTNLEPLLV GRPVDWNISP LPVVVGDSFL LQRALTNLLS NALKFTSTRE NARIAVWADE
HPDEWMVQVR DNGVGFDPRF AEKLFGVFQR LHRQEEFEGT GIGLALVRRI VLRHGGQVWA
DARPNQGATF AFTLPKRSLT AEERTQEDEI GVP
//
