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Database: UniProt
Entry: A0A158DEN9_9BURK
LinkDB: A0A158DEN9_9BURK
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ID   A0A158DEN9_9BURK        Unreviewed;      2010 AA.
AC   A0A158DEN9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AWB78_05077 {ECO:0000313|EMBL:SAK93059.1};
OS   Caballeronia calidae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777139 {ECO:0000313|EMBL:SAK93059.1, ECO:0000313|Proteomes:UP000071859};
RN   [1] {ECO:0000313|EMBL:SAK93059.1, ECO:0000313|Proteomes:UP000071859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29321 {ECO:0000313|EMBL:SAK93059.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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};
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DR   EMBL; FCOX02000031; SAK93059.1; -; Genomic_DNA.
DR   Proteomes; UP000071859; 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; 9.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 6.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; PF00672; HAMP; 9.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 10.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; 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; 3.
DR   PROSITE; PS50885; HAMP; 10.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SAK93059.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          196..253
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          293..345
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          385..437
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          477..529
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          569..621
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          661..713
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          753..805
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          845..897
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          937..989
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1029..1081
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1326..1559
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1625..1738
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1891..2008
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          1254..1316
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1674
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1941
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2010 AA;  216245 MW;  1541413231AC34DA CRC64;
     MNTISEEENT LIDSEFQMMV RTVAALREGE SVQKLPVDWT GVKGQLAAEL KMLADQCVRQ
     SSALGRAAGD AATGVRTSRG VDEEGLSGFW LQQARDSNEL LRASDTAHAC TRDIYAALIA
     LRKGEGASLA ADWPGLHGKL ADVFNDVVDQ NIRMSDELAR LSQAVGKEGR IYERATLPDP
     RGFWRRSIDS VNSLIVDLVH PTSEVARVIG AVAQGDLSKS MALEADGRAL EGEFLRTAKI
     INRMVEQLGT FAAEVTRVAR EVGTEGKLGG QADVKGVAGT WKDLTDNVNF MAGNLTSQVR
     NIAEVTKAVA AGDLSKKITV DVKGEILELK NTINTMVDQL RSFASEVTRV AREVGTEGKL
     GGQADVKGVA GTWKDLTDNV NFMAGNLTSQ VRNIAEVTTA VAAGDLSKKI TVDVKGEILE
     LKNTINTMVD QLRSFASEVT RVAREVGTEG KLGGQADVKG VAGTWKDLTD SVNSMGSNLT
     AQVRNIADVT TAVAAGDLSK KITVDVKGEI LELKNTINTM VDQLSSFASE VTRVAREVGT
     EGKLGGQADV QGVAGTWKDL TDSVNSMGGN LTAQVRNIAD VTTAVAAGDL SKKITVDVKG
     EILELKNTIN TMVDQLRSFA SEVTRVAREV GTEGKLGGQA DVQGVAGTWK DLTDSVNSMG
     SNLTAQVRNI AEVTTAVAAG DLSKKITVDV KGEILELKNT INTMVDQLRS FASEVTRVAR
     EVGTEGKLGG QADVQGVAGT WKDLTDNVNF MAGNLTSQVR NIADVTKAVA AGDLSKKITV
     DVKGEILELK NTINTMVDQL SSFASEVTRV AREVGTLGKL GGQADVQGVA GTWKDLTDSV
     NFMAGNLTSQ VRNIADVTKA VAAGDLSKKI TVDVKGEILE LKNTINTMVD QLRSFASEVT
     RVAREVGTEG KLGGQADVQG VAGTWKDLTD NVNFMAGNLT SQVRGIARVV TAVANGDLER
     KLTVEAKGEI AALADTINSM TDTLATFADQ VTTVAREVGV EGKLGGQAKV PGAAGTWKGL
     TENVNQLAAN LTTQVRAIAE VATAVTQGDL TRSITVEALG EVAALKDTIN EMIRNLKDTT
     ALNTEQDWLK TNLAKFSRML QGQKDLVAVG QLILSELAPV VGVQQAEFYV FGVVDQAASL
     RLVASYASDG HRSHGKQVEL GEGLVGQCAF EKRKILLAPS ASVDYRVESG LLSVVPQNVL
     VLPIVFEGQV KGVIELASIE RFNSTHLAFL DQLTESIGIV INTIEANTRT EDLLTQSQSL
     AQELQSRQEE LQQTNQELQE KARLLAHQNQ EVERKNSEVE QARQALEDKA KQLALTSKYK
     SEFLANMSHE LRTPLNSLLI LSDQLCKNPE GNLSGKQIEY SRTIHSSGND LLMLINDILD
     LSKIESGTVV LDVAEHRLAD MTTYVERTFR HVAEARNVDF VIHLDSDVPV SIVTDLKRLQ
     QILKNLLSNA FKFTHQGQVS LSIELALGGW GEDNEALNSA GSAIAFSVQD TGIGIPPDKQ
     QIVFEAFQQA DGSTSRKYGG TGLGLAISRE LSKLLGGEIR LTSVPEEGST FTLFLPRANE
     LVRTGRRKHA RRDGTGLTVL DVSSSTSHAR ADFATQPELA VEVPHEVAGA HIADDRNNIV
     QGDRVVLIVE NDVAFARVMV DAARQRGFKA LTTAFGAYAL MLVNQFKPDL ITLDLFLPDM
     EGWQVLARIK NDMATRHIPV CVISTDESRD RALRSGAFAF LPKPVESQAI LDDALASMAR
     YIEAKRRVVL VALSSVIERE LLSSALQGTQ AAVVFANSRD ALLPQLSSQP VDALVLADGI
     LGIAPEDIES ALASRESFAP LPVIVSAAGD VPPARWKHAR EGFIVQHAAS RDQLLDLSVA
     ALHIDAKRLA LEHGAILHAL RASQSALKDV KALIVDDDMR NIFALATIME DLGMRHVWAD
     NGRDAIRQVE SDPEIEIVLM DIMMPEMDGL ATMREIRRRP VGKALPIIAV TAKAMKGDRE
     KCIEAGAWDY LSKPVNRDDL LAVLRAWLHR
//
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