ID A0A0A0DS82_9BURK Unreviewed; 787 AA.
AC A0A0A0DS82;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JY96_16225 {ECO:0000313|EMBL:KGM41079.1};
OS Aquabacterium sp. NJ1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM41079.1, ECO:0000313|Proteomes:UP000029993};
RN [1] {ECO:0000313|EMBL:KGM41079.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM41079.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Masuda H.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM41079.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM41079.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Shiwa Y., Yoshikawa H., Zylstra G.J.;
RT "The draft genome sequence of a soil bacterium, Aquabacterium sp. strain
RT NJ1, capable of utilizing both liquid and solid n-alkanes.";
RL Submitted (OCT-2014) 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:KGM41079.1}.
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DR EMBL; JRKM01000001; KGM41079.1; -; Genomic_DNA.
DR RefSeq; WP_035039041.1; NZ_JRKM01000001.1.
DR AlphaFoldDB; A0A0A0DS82; -.
DR STRING; 1538295.JY96_16225; -.
DR eggNOG; COG5000; Bacteria.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000029993; 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 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; 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; IPR017232; NtrY.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGM41079.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029993};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..388
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 400..435
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 533..741
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 743..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 86270 MW; B2F7B5B36C24CA9C CRC64;
MSTIKANRWA WIVATAAIGG AGLIMSFLLV FATQNSERYE PHYQWLLWAN VALAAILILV
ILIAVARLAL RLRARKFGSK LLLKLAGIFG LVGLLPGLLI YTVSYQFVSR SIETWFDVRV
EGALEAGLNL GRSTLDNLTT DLANKTRLAA ERMSAPQPTA GLVGPAPATG VLELERLREQ
LGAQMVTVLS DSGQVEMTAG GDGTRILAAE RLPASWRQEA RSKGVMALVE GLDDRTEDKA
ERPREGPPPS VARVVALAWM PDHSFSLLAR GRYLMVTQKL QPELVRNALD VQTAYREYQQ
RSLGRVGLKR MYIGTLTLAL ILAVFGAFLL AAILGQQLAR PLLLLAEGVG EVARGDLRPK
AIFTSTDELG GLTRSFAAMT QQLADARTLV DRSVQELDSA RAHLQTILDN LTAGVIVFDS
TGRIDMVNPG ATRILRLPLS VYKGRYLSDV AGLEPFAENI RQRFELYATD PTPGERQQWQ
ESYELSLPSI PEPLTLLVRG AELPPNERLI VFDDLTEIVS AQRAEAWSEV ARRVAHEIKN
PLTPIQLSAE RMQMKLEDKL EDPSARQLLV RSVNTIVTQV QALKTLINEF RDFARLPTAK
LVPIDLNELV HDVMALYGHA LEHGTLQVEL GEGLPEILGD ATLLRQVVHN LVQNALDAIN
EHPSPDEPPR VLIRTDAPRK EDGSIRAVRL LVRDNGPGFP DKILKRAFEP YLTTKAKGTG
LGLAVVKKIA EEHGALVRLR NLGDSNDSIP KNGSELGYPS QGHTVRGAQV SLSFSKLSSK
TTQAGSH
//
