ID A0A0A0DQB5_9BURK Unreviewed; 814 AA.
AC A0A0A0DQB5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JY96_08685 {ECO:0000313|EMBL:KGM40083.1};
OS Aquabacterium sp. NJ1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM40083.1, ECO:0000313|Proteomes:UP000029993};
RN [1] {ECO:0000313|EMBL:KGM40083.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM40083.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Masuda H.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM40083.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM40083.1,
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:KGM40083.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRKM01000001; KGM40083.1; -; Genomic_DNA.
DR RefSeq; WP_035036671.1; NZ_JRKM01000001.1.
DR AlphaFoldDB; A0A0A0DQB5; -.
DR STRING; 1538295.JY96_08685; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 8929028at2; -.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12915; PDC2_DGC_like; 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; 4.
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; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE 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; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029993};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..380
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 383..435
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 509..561
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 582..802
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 550..582
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 814 AA; 90577 MW; C40155A278D5AB44 CRC64;
MVKTSRLGLV ALNVMMTVFC ATTLWRSWQA DMAAGKTQAL TTARLLEQGA TASFDKIAVV
LSGVADRLEH EATEGAQESG TNLWQTVDQA ISRIPDVQQI EVFDANGQQL CGQPMQRCMH
LDISAQDYFQ RLLKQPDERV GFYGTYTSLA DGQPCVIMAR ALFRAPHAFN GVIIAVIPVS
RLSSLIAKAS LGQHGIAALR SSTLNLVVRY PAAPPSASLA NQLTTELTRV IQSAPNEGVY
RSTSQLDGVE RVIAYRRMPD LALYVMVGNA LDDFMADWWW HLAWMIAFLL TFFTASWSLS
RRTLRRARQY ERTQRLYNTA PCGYHTLDPH GRYLSINDTE LTWLGCPRDE VIARLSPTDF
MTEESRQTFA QNFPAFKQKG ELNGLELELV SRQGVVRRVL VSAKAVQDKQ GQFTMSNSVM
HDITPLHQAR QALREQARQQ ALMLNTDLIG IMRLVQRKTV WANQGMTRIF GYPGEAWQGM
PVRQLHADEA SYAHVGEEAY AAFRQGRPYR TQLQMRRMDG SLVWIDVSAA RLSDTTEEVM
LLLADITPLK EAEQARLKAV ELEAQNQQLR ALSRLKDDFL ANMSHELRTP LNAIMGFTQL
LQMQRYAPDS ALYGSALHQI ESGGQRLLDL VESMLAFGQV EAGKMPFSPA MIDVQAALDD
ICDTVRPQAQ QHQIELHTAI DPTMSKVEVD PLRLRQMGVA LASNAIKFSR PGSLVWVRAG
YLGELEWFLE VEDQGAGIAA SDLSRLFTPF VQLSSGMSRT HEGAGLGLAL VRHMARAQGG
EVYLLTQEGV GSIFRIVLPR QAPVPADAWA SANI
//