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Database: UniProt
Entry: A0A1G7PZG1_9BURK
LinkDB: A0A1G7PZG1_9BURK
Original site: A0A1G7PZG1_9BURK 
ID   A0A1G7PZG1_9BURK        Unreviewed;       670 AA.
AC   A0A1G7PZG1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN05216320_1023 {ECO:0000313|EMBL:SDF91608.1};
OS   Duganella sp. OV458.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1855290 {ECO:0000313|EMBL:SDF91608.1, ECO:0000313|Proteomes:UP000199454};
RN   [1] {ECO:0000313|EMBL:SDF91608.1, ECO:0000313|Proteomes:UP000199454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV458 {ECO:0000313|EMBL:SDF91608.1,
RC   ECO:0000313|Proteomes:UP000199454};
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};
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DR   EMBL; FNCD01000002; SDF91608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7PZG1; -.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000199454; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SDF91608.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:SDF91608.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          300..372
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          375..427
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          447..665
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   670 AA;  74491 MW;  E83F65A5CE724906 CRC64;
     MTTEPTQAPA PRRRPLSNTS LRWLLPIMLV LFFLAILIWL PWQARQMESN ERQEQLIADT
     LWVEQTIRFQ MARDEESLRS LGVEISAGNL NTRQLHERMA RLLKNGQELV RVVWLKPNGE
     LAATSDPLAN PVELSPASRE TADITRKTHR PMYTQPEAQT QVANAAPSAV LMDYHVPLFR
     GDEYLGDLMA TFQTSALLDE MVPWWFAQDN QVSLVDRDDK VLARRAAAGP GHGVYTHKRA
     LDLPGASVML VTDSVKSEPK LLPNLLVGSV IVLSLGLLWS LLALWGHISK RLAAEGALRQ
     QMLFRTAMEN SLVTGLRARD LEGRITYVNP AFCQIVGYPA EEIVGKLPPM PYWATEAMSE
     YEARFASVLA GKVTPQFETF FQRPNGDRVP VLVFEAPLVD NNGKQTGWMG SILDISDRKR
     IEEVNRQQQE KLQASARLAT MGEIASMLAH ELNQPLAAIS SYTTGALNVL DRDGPLDRSI
     LKPALEQAST QAQRAGQIIR SVHEFVKKRE PLRQAVAIAS LLDGIRALIE LQARQSYVSY
     RTEIPPDLPP VRADRVMIEQ VLLNLTRNGI EAMQHVQPQR RILKVVADYD AVTAQVSVAV
     IDQGHGIPEE VAARLFSPFF STKAEGMGMG LNICRTAIEF HGGALTFRAN PQGGTIFTFV
     LPAATEQETS
//
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