ID A0A158GEW2_9BURK Unreviewed; 794 AA.
AC A0A158GEW2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWB64_02726 {ECO:0000313|EMBL:SAL30668.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL30668.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL30668.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL30668.1};
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; FCOC02000006; SAL30668.1; -; Genomic_DNA.
DR RefSeq; WP_060819604.1; NZ_FCOC02000006.1.
DR AlphaFoldDB; A0A158GEW2; -.
DR OrthoDB; 5389366at2; -.
DR Proteomes; UP000054893; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SAL30668.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:SAL30668.1}.
FT DOMAIN 14..71
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 89..141
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 142..196
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 217..269
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 289..512
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 532..648
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 679..793
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 582
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 728
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 794 AA; 86233 MW; D1F61B8F3DB55590 CRC64;
MTLNTSGSLG DVNSEHRYEL LVTSVSDYAI YMLDPTGHVV SWNTGARRFK GYEKDEILGQ
HFSVFYTEED RVAGKPALAL STAQADGRFE GEGWRVRKDG SRFWASVVVD RIIDATGTFV
GFAKITRDIT ERKAAHEALR VSEEQFRLLV QGVTDYAIYM LSPTGEVTNW NAGAARIKGY
TDKEVIGTHF ERFYTEADRA SGLPARALAA AKRDGRFEHE GWRVRKDGST FWAHAVVDII
RDGTGRHIGF AKVTRDITER KHAAEALERA NAALAQSQKM EAIGRLTGGV AHDFNNLLQV
ISGNLQLLAQ DVAGMGRPEQ RVRNALAGVT RGAKLAAQLL AFGRRQPLAP KVVNLGRFIR
NLDDMFRRAL GDGIQVETVV SGGLWNTFVD PYQVEHAILN LAINGRDAMQ GHGRLTIEAG
NAALDDNYVR SNPGAETGQY VMVAVTDTGS GIAPDLMERV LEPFFTTKPE GQGTGLGLSM
VYGFVKQSGG HLKLYSEVGH GTTVRIYLPR ALQEEDTVVE IDAGPVTGGS ETILVAEDDE
DVRRTVVELL SNLGYRILLA KDAMSALAII ESGVPIDLLF TDVVMPGSLS SPELARKARE
RLPSIGVLFT SGYTQNAIVH GGKLDPGVEL LSKPYSREAL ARKIRHVLRN QEQREAAAAA
LSAAKPATAH LPAAFASQQV LLVEDDDLVR AGTIEMLNRL GIAPLQAANG AAAMSVLEAQ
PVDVLIVDIG LPDISGIDLA INASSRFRQL RIVVASGYDI VLSPEQRTML PTARILRKPY
DALDLSRVLG SHSD
//
