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Database: UniProt
Entry: A0A126ZA95_9BURK
LinkDB: A0A126ZA95_9BURK
Original site: A0A126ZA95_9BURK 
ID   A0A126ZA95_9BURK        Unreviewed;       560 AA.
AC   A0A126ZA95;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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=AX767_03535 {ECO:0000313|EMBL:AMM23524.1};
OS   Variovorax sp. PAMC 28711.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM23524.1, ECO:0000313|Proteomes:UP000070169};
RN   [1] {ECO:0000313|EMBL:AMM23524.1, ECO:0000313|Proteomes:UP000070169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM23524.1,
RC   ECO:0000313|Proteomes:UP000070169};
RA   Park H.;
RT   "Complete genome of Variovorax sp.";
RL   Submitted (FEB-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; CP014517; AMM23524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A126ZA95; -.
DR   STRING; 1795631.AX767_03535; -.
DR   KEGG; vaa:AX767_03535; -.
DR   Proteomes; UP000070169; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 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   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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AMM23524.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070169};
KW   Transferase {ECO:0000313|EMBL:AMM23524.1}.
FT   DOMAIN          29..84
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          102..154
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          151..199
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          224..278
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          303..521
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          526..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          269..296
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   560 AA;  61162 MW;  7FE7AF5B13D2ACFD CRC64;
     MPPKLPSDVL RQAAALQDAI FNSEMFSKIA TDADGVIQIF NVGAQRMLGY SAAEVINRIT
     PADISDPAEL VARARALSEE LATPIAPGFE ALVFKSCRGI EDIYELTCIR KDGSRLPVVV
     SVTALRDPAD AVIGYLLIAT DNSARKQAEA AKREHDALLQ TIHLHSIVSV TDRSGRIIEV
     NDGFCRISGY SRAELLGQTH GIVNSGVQKE AFWIDMWRSI TAGRPWRGEI CNRAKDGSLY
     WVDSVIAPFL DDAGKTKNYI SIRTDVTDRK EAEAARQTLN EHLAAAMQAA EKANQAKSDF
     LSSMSHELRS PLNAILGFAQ LLDSGTPAPT PSQKESIDQV LLAGWYLLAL INEILDLSLI
     ESGKLSLSPE SMALADVLND CQAMIEPQAR KGSITLVFPA FDAPHFVKAD RTRVKQVFVN
     LLSNAIKYNR PGGAVMVDCH DTGAGRVRVT FKDTGEGLSQ DKLAQLFEPF NRLGQEAGPE
     EGTGIGLVVS KRLIELMGGT IGVASTVGVG TTFWIELQRP ARRNSIRGSH DWDRRRPHPP
     TRRHRDRPCS ASKTTRPTCC
//
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