ID A0A158GNK0_9BURK Unreviewed; 796 AA.
AC A0A158GNK0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWB65_02196 {ECO:0000313|EMBL:SAL32970.1};
OS Caballeronia humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL32970.1, ECO:0000313|Proteomes:UP000054977};
RN [1] {ECO:0000313|EMBL:SAL32970.1, ECO:0000313|Proteomes:UP000054977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL32970.1};
RA Oliw E.H.;
RL Submitted (JAN-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};
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DR EMBL; FCNW02000008; SAL32970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158GNK0; -.
DR STRING; 326474.AWB65_02196; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000054977; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SAL32970.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SAL32970.1}.
FT DOMAIN 4..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 374..515
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 517..651
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 674..790
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 168..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 175..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 723
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 796 AA; 86957 MW; BD810DD434BD2E4B CRC64;
MTSGDTIPPS LIELFCEEAR TQAQILSDGL LALERAPREP VTLEACMRAA HSLKGAARVV
GVPVGVTLAH VMEDCFVAAQ EARLTLDAGH IDMLLRGVDL IVQIGMTRGA EEEAQLERNA
DAFAAELSAR LEGTAALAPA HDRLAISPVG TNAKAAAPFD LSSELTLPAV SVSAPDRSEE
REEREEREER EEREERDEPA EPAYNAPSGP RMLRVRADTL DRLLSHSGES LVESRWVKPF
AQSMLRVKRI QRDANRALER LHETLADVPE YQQLDPRARA ALDEARQLSA EVHRHLNERL
AELENFDRRS THLSQQLYDE ALECRMRPFV DATGGFARMV RDVARSLGKE ARLVIVGEST
QVDRDILDML DGPLGHLLRN AVDHGIEPPS VRRALGKPAE GTITLEARHS AGSLFISVTD
DGAGIDIDAL RRVVVQKALA SEATAARMSD VELSEFLFLP GFSMRDTVTD VSGRGVGLDA
VQDAVRQVRG SVRVIHDAAQ SHTGTRFLLQ LPLTLSVIRS LIVEVAGEPY GLPLAHVTRT
MVLPASAIDM LEGHQHFSFD GRRLGLVTAH QVLQAGTFDA TGDQFNIVVI GQGAVSYGIV
VDRFLGERML VVQPLDKRLG KVRNIAAGAL MENGDPLLIA DLDDWLRSVE KLVAGGEIGR
VGAGAARTEV AAKRVLVVDD SLTVRELEKK LLVSRGYDVT IAVDGMDGWN AVRGERFDLV
ITDIDMPRLD GIELVSLIRR DAQLSNLPVM IVSYKDRAED RQRGLDAGAD YYLAKGSFHD
QTLLDAVRDL IGEAKS
//
