ID A0A257H3V0_9BURK Unreviewed; 1662 AA.
AC A0A257H3V0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CFE44_08135 {ECO:0000313|EMBL:OYU45317.1};
OS Burkholderiales bacterium PBB4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015566 {ECO:0000313|EMBL:OYU45317.1, ECO:0000313|Proteomes:UP000216392};
RN [1] {ECO:0000313|EMBL:OYU45317.1, ECO:0000313|Proteomes:UP000216392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB4 {ECO:0000313|EMBL:OYU45317.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-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 -!- 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:OYU45317.1}.
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DR EMBL; NKIJ01000167; OYU45317.1; -; Genomic_DNA.
DR Proteomes; UP000216392; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 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; 4.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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); 4.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000216392};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..381
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 469..515
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 541..595
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 615..656
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 669..723
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 743..797
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 800..852
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 928..980
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 991..1212
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1234..1357
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1386..1504
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1549..1647
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1288
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1437
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1588
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1662 AA; 179644 MW; 441039BED920BF9F CRC64;
MRHSCARAVS MQSGFTARVE TLRRLCYSVP GGRPAHFTIA CMKNSFNPVR LFLEILLVLA
IAHAAILVTL PYLGQPTGGQ LGWVSLVLLS LVAAPAVFWR CLMASRSQEP DQGATTSSSS
RLRMRNAIAL TAGVQALGLL ATVGGVYWLK QTLDLESSLR FVRIADRLEE EVKRRFDMPL
AALNAARGVY AVKPQLNRQE FRQYVESRDL ARELPGIRGI GFIERVPRAG LAAFEARERA
DGAPDFKVTT SGTSQDMLVI KFIEPMVGNA QAWGFDAGQE AFRRSAAQRA LATGEPSMTA
RLNLLQDQAK TTEFLYFMPV YRRGSDPVTQ AQREAALVGL LYTPFVAKEL LGTVMSQVEP
SVDFDLYDGA AVHADHLIFD ADGHVNAATA STADPDRPQV ALRTLQVAGR TLTLRISSLP
AFFAAQDRSG LVMAAIGGTL GSFLMALTVW LLAAGRIRAQ RLADRITGDL NRMARVVKHT
HNAVILADAG MKITWVNDGF TRLTGFSLAE ALGKTPGELM GKSEASADAF AKVEAALAKG
EACRALLVNR VKGGREVWMD TEIQPTLNEA GQLIGFMEIG TDVTAQIEVQ RKLETAIRDS
NALLSTVEMH AILSVTDAQG TITEVNDAFC EVSGYDAEEL IGQNHRLLKS QGHPADFWPQ
IWASVSIGMS WRGDVCNRAK DGHLYWVDSM ITPFIGDDGA VQKYVLVGTD ITARVLDQQR
LAAMSDRIAL AIEGGNDGLW DWVDVSHDAQ WWAPNFYAML GYAPEDMVAS ASSYRALLHP
DSRAVSDAAN QHALATHEPL DVEVQLLTKH QGYRWFRGRG KVFVDASGKA ARMAGATQDI
HDRKVAEAHA LATSRRFALA ADSGGIGVWE WDVATASLHW DAKMFQLYQR TQDGEVVAHQ
VWRESVHPED LPRCKAELAA VLAGEQAYDS SFRIFWPSGE VRHLRSAARV IRNADGIATG
MVGVNFDMTD VVHAAEVAEE ASRAKSNFVA NMSHEIRTPM NAILGILKLL QNTELNVRQQ
DYVAKTEGAA KSLLGLLNDI LDFSKVEAGK MTLDPRPFRV DHLLRDLSVI LSANVAQKPV
EVLFDIDPAV PPCLVGDDMR LQQVLINLGG NAIKFTAQGE VVLQLKVLDH QADTVLLEFA
VQDSGIGIAP ENQAHIFSGF SQAEASTTRR FGGTGLGLAI SSRLCALLGG ELKLHSVVGQ
GSTFYFQARL AVAAPEALPA LPAAQGVPLE SDLRVLVVDD NPVALELLAR AARSLAWAVD
TASSGAEAIT LVQNALNAGH AYQAVFVDWQ MPEMDGWEVS QRVRALSDSD APMVMMVTGH
GREMLGQRSV RDQTLLNGFL VKPVTAQMLR DSVRDARAAH AMAEAGHNPA APQVVVSTPK
RLQGLRLLVV EDNKINQLVA HGLLTKEGAD VTLADDGQQG VQAVLQASTP FDVVLMDIQM
PVMDGYTATR TLRERPELQS LPIVAMTANA MASDRAACLA AGMNDHVGKP FELDHLVATL
LHYSGRNPLP EKELVDASVP PAASVPPPAE AAAIAPMDVE DAIERIGGDA ALYADVLQTF
AADLKGLPAR FAAHLAADRG TDCIRDMHTQ KGLAHTVGAM HLAAVTTKLE RRCKRALTPG
DHAPMVAELQ SAVDITLEQV APVLQRYGLV QPEAIGGAVA PD
//
