ID A0A0A0DQN1_9BURK Unreviewed; 1125 AA.
AC A0A0A0DQN1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JY96_12250 {ECO:0000313|EMBL:KGM40549.1};
OS Aquabacterium sp. NJ1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM40549.1, ECO:0000313|Proteomes:UP000029993};
RN [1] {ECO:0000313|EMBL:KGM40549.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM40549.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Masuda H.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM40549.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM40549.1,
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KGM40549.1}.
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DR EMBL; JRKM01000001; KGM40549.1; -; Genomic_DNA.
DR RefSeq; WP_035037772.1; NZ_JRKM01000001.1.
DR AlphaFoldDB; A0A0A0DQN1; -.
DR STRING; 1538295.JY96_12250; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3300; Bacteria.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000029993; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR005330; MHYT_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF03707; MHYT; 3.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
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 SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00244};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000029993};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244}.
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 58..81
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 22..219
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 270..340
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 397..473
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 476..528
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 546..762
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 784..903
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 935..1034
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 833
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 976
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1125 AA; 122037 MW; 25132D865B686D37 CRC64;
MSVLSPFFVW QTDPSLLLYG SYDPWLVALA LAVSVFSSTM GLQAAAQAGE MPTRSMRQLT
LLAGSLALGC GVWAMHFIGM LSFKLCTTVH YDAQLTMLSI VPSAVASWVA LDLLSRARVS
KAQLWLGGTL VGAGIGTMHY MGMAAMQMPI ALRYDPLMFA LSIVVAVSLA VLALWVRFGV
KDSVLGMQSR LVQSMISGSV MGLAISGMHF TGMAAARFIG KPLGNGSNAL QDPVAIALSI
TLVTMVATVL VAGATGLSRY RQLIERLESQ GARLRAISNS ALDGIIVFDS QGTIQDFNPG
AQRIYGWAAH ELIGQHVSRL MPPKRKALAE TDFDAFLREA SRFIDEERDT EGWHRDGHLI
PIRLVMARMR ITGANLYVAF VSDITERMRM ARELQDSEEQ FRTLIANIPG ISYRCRMEPG
WPMVFISDAV EKITGFPAGD FLGPMASVRF TDLVPEEDVA RIAAVVRESL RQNRHFVLEF
QLRHRDGSLR WMWGNGSVVG SKDGTVDWID GVLLDITERR QMEEDLRVAK ERAEAAAQAR
STFLANMSHE IRTPMNAIMG FTDVVLSGDL QAEQRKRLET VHKSARSLLH LLNDILDTSK
LEHGAVELEH LDFSLTDLVQ QLCAEQSVQA KRKHLSLHGE VDASVGDYVK GDPHRLRQIL
LNLVGNAIKF TEAGRVSVRA QREAEGVHFM VQDTGIGIAP DRLPHIFDAF TQADASMSRR
FGGTGLGTTI SKQLTELMHG RIWATSEPGQ GSVFHVLIPL EPGDAARAQG LTHPAINMAL
PPMRVLAVDD VEQNLELITV LLSKQGHSVT TASNGEQALA CAAQGEFDLI LMDVQMPVMD
GLSACRALRQ RELQQGARRT PVLALSASVL QEDRQATIDA GMDGFATKPI EMGELMAEMA
RVTGLTLIPI QAAAPTAAGV QADAAIVDLP RGLQLWQAWP AYLQALQRFA SDRSSWLAAQ
QQAPVPDNEV AFSEAHRLKG AAGNLGLIQI EQAALQVETL ARQPAGEALA SAWQALLNSL
AAATQEIAHL AAQSPGPNLA TPPAVEMDVA TLHRKLGQLK AAFQRGECLD NLLTKVQQAC
APYADASKLS ALAEAVEAFD FDAAARCTQD IADGLLQLET PDAPL
//
