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Database: UniProt
Entry: A0A1V3RRJ1_9BURK
LinkDB: A0A1V3RRJ1_9BURK
Original site: A0A1V3RRJ1_9BURK 
ID   A0A1V3RRJ1_9BURK        Unreviewed;       661 AA.
AC   A0A1V3RRJ1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B0E41_23525 {ECO:0000313|EMBL:OOG79484.1};
OS   Hydrogenophaga sp. A37.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG79484.1, ECO:0000313|Proteomes:UP000189189};
RN   [1] {ECO:0000313|EMBL:OOG79484.1, ECO:0000313|Proteomes:UP000189189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37 {ECO:0000313|EMBL:OOG79484.1,
RC   ECO:0000313|Proteomes:UP000189189};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOG79484.1}.
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DR   EMBL; MUNZ01000178; OOG79484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3RRJ1; -.
DR   STRING; 1945864.B0E41_23525; -.
DR   OrthoDB; 8552871at2; -.
DR   Proteomes; UP000189189; 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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 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; IPR033417; CHASE8.
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; 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; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF17152; CHASE8; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189189};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..228
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          238..278
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          322..374
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          403..621
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          365..396
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   661 AA;  73239 MW;  37FCC8E6BD3F5EE6 CRC64;
     MFRQLNIHKR LTFVLWGTAV LAFVVAGVGL LLYQSYTREH RARQIMEPYA QLVAVGTDAA
     VAFADPVRAQ EILDTLRANP QILEADIFLD DGRLLANFNR VSDARPQPLA EQPDGLYLGA
     DATQLLQTLP KGGRLRISMN LEQLSEQTHQ VMWLFGAAML VLLAATLAQM AVLRRTIARP
     IASLTEATER VRAGADYTHR IPVSGDDELA RLGQSFNAML DGIQQREDDL RRLAAFQRTI
     LTNAAYGIIS VAPDGTVTSF NPAAERLLGY AADEVAGKHM PALWHDPQEV AQHAQYLSSE
     LGETITSGFE VFAARPRRGL TEEREWRFTR KDGTRFSASL SVTALRDAGG RITGFVGLVY
     DLTERKQVEA EIHKLNQELE QRVAERTAQL TEANKELEAF AYSVSHDLRS PLRHIDGFLG
     LLREQFPVAL DAQSERYMDT ISKAVKRMGE LIDDLLSFSR MGRQEMTKAP VDLGALVKEV
     IHEFEPEAEH RAIDWHIGEL PVVFGDGAML RVVLANLISN ALKFTQTRQQ TIIEIGCLPV
     QSGHENQTVV FVRDNGVGFD MRYANKLFGV FERLHSLKEF EGTGIGLANV HRVVSRNGGT
     TWAEGKVDGG ATFFFSLPRE KPTAAAQIIP SKPTESPSCS DCEGLVAHVG SEKRCPLHPL
     Q
//
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