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Database: UniProt
Entry: A0A068YUV4_9BURK
LinkDB: A0A068YUV4_9BURK
Original site: A0A068YUV4_9BURK 
ID   A0A068YUV4_9BURK        Unreviewed;      1460 AA.
AC   A0A068YUV4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
OS   Polaromonas sp. CG9_12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS55145.1, ECO:0000313|Proteomes:UP000043372};
RN   [1] {ECO:0000313|EMBL:CDS55145.1, ECO:0000313|Proteomes:UP000043372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Smith H.J., Foreman C.M., Ramaraj T.;
RT   "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT   Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT   Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 2:1-2(2014).
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};
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DR   EMBL; CCJP01000005; CDS55145.1; -; Genomic_DNA.
DR   STRING; 1504672.gene:199034410; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG0840; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9796305at2; -.
DR   Proteomes; UP000043372; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 5.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 2.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 3.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF18947; HAMP_2; 5.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 5.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR   PROSITE; PS50885; HAMP; 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          100..157
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          197..249
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          289..341
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          381..433
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          473..525
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          771..1005
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1073..1186
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1195..1311
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1341..1458
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1005..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          692..761
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1023..1037
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1122
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1244
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1391
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1460 AA;  159393 MW;  D10F2790342E7FD1 CRC64;
     MATPQQTLSD EINLKQLLTV LDAYRKGDFS ARMPNDLVGL PGKVADTLND IIDRGVETTT
     EFGRVAQLVG KQGKLDERIK LPSMKGSWAK LVDSSNALAN DLVSPLNEMI RVVGAVAKGD
     LSQNVPTEID GLKLQGQFLK SAQIVNTMVT QLGTFSSEVT RVAREVGTDG KLGGQAEVRG
     ASGTWKDLTD NVNAMASNLT NQIRNVAEVT TAVAKGDLSK KITGDVKGEI LVFKNTTNAM
     VDQLSAFASE VTRVAREVGT DGKLGGQAAV IGVAGTWNDL TENVNRMASN LTNQIRNVAE
     VTTAVAKGDL SKKITGDVKG EILVFKNTTN AMVDQLAAFA SEVTRVAREV GSDGKLGGQA
     AVIGVAGTWN DLTENVNRMA SNLTNQIRNV AEVTTAVAKG DLSKKITGDV KGEILVFKNT
     TNAMVDQLAA FASEVTRVAR EVGSDGKLGG QAAVIGVAGT WNDLTENVNR MASNLTNQVR
     AIAEVVPAVT KGDFTRSVQV EAKGEVADLK DNVNQMIGAL RETTRQNSEQ DWLKTNLAKF
     TRLLQGQRDL TAVSKMVLSE LAPLINAQHG VFYMMDETVA DNPRLKFLSA YAFTERKNLA
     NEWRVGEGLV GQCAYEKQRI LLTNVPSDYI QITSGLGGSK PQNIVVLPIV FEDKVKAVIE
     IASFTLFSQT HQTFLDQLGE SIGIVLNTIE ANVRTEELLK QSQSLAAELQ SQQEELRQTN
     EELEEKAKLL EDQKVEVEYK NRQIEASKLT LEEKAEELTL TSKYKSEFLS NMSHELRTPL
     NSLLILSQQL AENAEHNMSE QQIEYAKTIQ GSGKDLLALI NEILDLSKIE SGTVTPDLQD
     VSFANVREQV ERTFRHVAES RGLGFGVEFA PGLPSSLYTD SQRLQQVMKN LLSNAFKFTA
     KGQVSVRIEP VESGWSVDHD GLNRAQTVIG LYVTDTGIGL PTTKQKIIFE AFQQADTGTA
     RKYGGTGLGL SISREIARLL GGELRLATSS PGKGSTFVLY LPLRASEPGQ NSRGTPGGAP
     DSGKRQRLER DGESFAPKAA RPDPAAQEVP EGRMPPATAV ADDRAAIQPG DRTLLIVEDD
     ARFADILLRA ARDKGFKGIV AARGDDGIKL AGEFKPTAIT LDLHLPDMDG WVVLERLKRN
     PDTRHIPVEI ISAEDNRLRG LRYGAFEYLV KPVTAESLQK ALADVNKFAE REVKDLLVAD
     GDEQHLKNVL DLIGSGDVRI KSVASGKDAL AALKKKRYDC IVLDLKLPDI PVADLLEAIQ
     GFDLTRDVPV IIYGMNELPQ QEQERLKSLA LKGIIKEVRT PERLLDETAL FLHRVVSKLP
     DERRQMLETL YLSADSLAGK KVLVVDDDVR NIFALTAVLE RHKMAVIVAE NGRAALEELG
     KNPDVHIVLM DLMMPEMDGF ETMRQIRKMK QFESLPMIAL TAKAMKGDRE KCIEAGASDY
     VSKPVDTDQL LSLLRVWLYR
//
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