ID Q47JH8_DECAR Unreviewed; 1066 AA.
AC Q47JH8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Daro_0244 {ECO:0000313|EMBL:AAZ45003.1};
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ45003.1};
RN [1] {ECO:0000313|EMBL:AAZ45003.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCB {ECO:0000313|EMBL:AAZ45003.1};
RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT "Complete sequence of Dechloromonas aromatica RCB.";
RL Submitted (AUG-2005) 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; CP000089; AAZ45003.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47JH8; -.
DR STRING; 159087.Daro_0244; -.
DR KEGG; dar:Daro_0244; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4564; Bacteria.
DR HOGENOM; CLU_000445_133_1_4; -.
DR OrthoDB; 9813903at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR004010; Double_Cache_2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR033480; sCache_2.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08269; dCache_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01049; Cache_2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:AAZ45003.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AAZ45003.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..455
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 482..534
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 535..605
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 607..661
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 697..918
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 947..1063
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 996
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1066 AA; 119341 MW; 368C0433E167BD4A CRC64;
MNLIKGRRRV RLTADEKTVP RIHLIGTLLT VLVLTLALGG FFSWQSLSEQ RAAFARVELA
ATQQLEARLQ AEMDGVTNFI EFTRSRTEDV LRRSLTEQVD TAYQIVESIY AQEARRRPPA
EVKRLIIEAL RPARFYEGRG YYFIDDMQGQ FILLPTAPQL EGKTILDNRD DTGHYIMRGL
IEAARQPRDE GFSRYRWYRP DDATQMADKL AYVRHFAPYD WLIGTGDYTY KWEALQQKEA
LARLRALHFG QSGRFGVLDG SGRNLLSPSD RALDGMLIHD MAAPEKAALE KLLAAGERGG
GFVRYQWLNP ENGQLVNKTA LVNVVKPWNW FVVATTFDDD FQSLLGEELR KHEAGHDQRL
LNLLIAIVAA LGLGLLSSLL FSRWSKRLFA DYHQQRLAQE AALRVQADEL KVLSRAIEQS
PVSIVITDTG GCIRYVNPKF EQVTGYTSQQ VLGQNPRILS SGEKSPDEYR ELWRTIKSGQ
TWQGEFHNRR QDGSLFWERA SISPIIDEQG QILHFLAVKE DISEHKQIEE ALRVSEYKMA
TILDSVEAYI YIKGTDYCYQ YANRRVCELF AREMNGIVGH QDTEFFDPAT CANLRRNDRR
VIEQGERVVE EEVNRTVDGQ ITSAFLSIKI PLRDQDGQIY ALCGISTDIT VRKQAEAELE
HYRQHLETLV QSRTVELARA KDAAEAANRA KSSFLANMSH EIRTPMNAIM GLTHLLQKDV
LDSRARERLG KIGESANHLL NVINDILDLS KIEAGRLALE IREFSPEAVL RQTISMLDER
AAAQGLRLTS HLASDVPALL CGDAVRIGQA LLNFVGNAIK FSERGEIALR ARVDRRDGEQ
VMLRFEVQDQ GIGMDAGQQA RLFQSFSQAD DSTTRKYGGT GLGLAINRHL ARMMGGDVGV
DSALGVGSTF WMTVCLAVAT RQPEALAADA AAVAPESQIA RLYGGRRVLL VEDEPINQEV
AAELLSLAGL VVEVAVNGAE AVERVRHGTY ALVLMDMQMP VMGGLEATRL IRQLPGKAVL
PVLAMTANAF DEDRQACLDA GMNDHIGKPV DPDLLYASLL RWLAHG
//
