ID A0A1G6K8M1_9BURK Unreviewed; 832 AA.
AC A0A1G6K8M1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444679_102112 {ECO:0000313|EMBL:SDC27218.1};
OS Variovorax sp. CF079.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDC27218.1, ECO:0000313|Proteomes:UP000198763};
RN [1] {ECO:0000313|EMBL:SDC27218.1, ECO:0000313|Proteomes:UP000198763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF079 {ECO:0000313|EMBL:SDC27218.1,
RC ECO:0000313|Proteomes:UP000198763};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMZU01000002; SDC27218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6K8M1; -.
DR STRING; 1882774.SAMN05444679_102112; -.
DR OrthoDB; 5519028at2; -.
DR Proteomes; UP000198763; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000198763};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 346..398
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 604..827
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 383..410
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 832 AA; 90420 MW; F0D661D6C29FA001 CRC64;
MKAPAAWTSL GFRGNAPSAV EMKAAEEDGR AMPDVALPAE SARDIHRGHL FRKYLLLILS
LVMAVLLASG AISLYFSYQE NKAALASLQQ VKAVGAASRI EQYIQQLTEQ LSFASVPLFD
EADLEARRIE FLRLLRQVPE VTDVAQLDGS GLERVAVSRL GMDSVGSGKD RSSEAPFQHA
RAGSPWFGPV YFHKDTEPYM TVAIRSEGDK SAVTVADLNL KFIWDVISRI STDDAGKAYV
VDRNGLLVAD PDIGLVLRKT SLASLPHVRA AAAAKAPGPQ AMVTHDLQGA QVLVSVAPIE
PLGWNVFVER PMAEVYAKLN ASILRTGLLL LAGLMVSAVA AWVLARNMVR PIRTLAAGAR
RIGEGELDAQ IVVKTGDELE ALADQFNRMS AQLRESYGEL ERKVEQRTAE LTASLEFQTA
AAEVLRVLSH TPSDLQPALQ AIAERSVLRC RADASKIWLQ EGDHFRAVTG YPVKGGSGPG
RDDALPMSAR SVVGRAFVEG RTVHVEDVAQ LVDWRPPASR KAPKRNDVHT VLAVPMVREG
ASIGIIAVLR KEVQPFSDAE VRLVETFADQ AVIAIQNARL FREIENKGRE LEVANRHKSE
FLANMSHELR TPLNAIIGFS EVLTERMFGE VNDKQMEYLQ DIHSSGQHLL TLINDVLDLS
KIEAGRMELD LSCIDLGLLM DDALTLVRER AQRDGVLISL EIGDGLTEWV ADARKVKQVV
VNLLSNAVKF TPAGGSVRLR ARRLDAAGQS VAEVSVADTG VGIAPEDQAL VFDEFRQAGS
DALRRAEGTG LGLALAKRFV ELHGGTIRVE SRPGEGATFS FLLPMQVPEA VI
//