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Database: UniProt
Entry: A0A2S9KHM6_9BURK
LinkDB: A0A2S9KHM6_9BURK
Original site: A0A2S9KHM6_9BURK 
ID   A0A2S9KHM6_9BURK        Unreviewed;      1333 AA.
AC   A0A2S9KHM6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C6P61_03475 {ECO:0000313|EMBL:PRD69951.1};
OS   Malikia spinosa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Malikia.
OX   NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD69951.1, ECO:0000313|Proteomes:UP000238326};
RN   [1] {ECO:0000313|EMBL:PRD69951.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=83 {ECO:0000313|EMBL:PRD69951.1};
RA   Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT   "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT   mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT   serpentinized springs.";
RL   Submitted (MAR-2018) 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:PRD69951.1}.
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DR   EMBL; PVLR01000008; PRD69951.1; -; Genomic_DNA.
DR   OrthoDB; 5290456at2; -.
DR   Proteomes; UP000238326; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00088; HPT; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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; 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; 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   InterPro; IPR001638; Solute-binding_3/MltF_N.
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; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00062; PBPb; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        263..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          299..369
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          373..425
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          524..575
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          593..814
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          832..953
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          980..1096
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1162..1256
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          409..436
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          560..589
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         886
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1029
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1201
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1333 AA;  147158 MW;  2AA963A97E8CD0AC CRC64;
     MSLRSEFKRA GSQLLLALLL SGLPWAAWAT HAVRVGVYEN EPKIFSDANG QLSGIFGDLI
     NEIARREGWT VVPVPCAWED CLNALQEGGI DLMPDVAYNE ARARLFDFHQ VPALHSWSQL
     YRHEGVSIVS MTDLQGRRVA VLDGSVQQEY LSAMLDGFGL RTELVPVPSL HEGFARVESG
     ELDAVAANHH FGDRNARAHR LQETPLMFQP SRLFFATGQG RNAELLAAID QYLQPWQSEP
     SSIYFTVLKR WGLPPTPSQI PRYLWWSLFS VATLLALALG LAAWLRREVA RQTRSLRASE
     DKLATILNSV DGYIFIKDTQ LRYQYVNQKV AELFGRPAAA IVGCSDEEFF DAATVQTLHE
     IDRSVIDGGM RVAGEEVNAT RDGRGSRLYY VVKQPLREPD GRVYALCGIS TDITELKQAQ
     AELERYREHL QQLVNERTVE LETATAALRE AGAEQLAIFD AATAGLMAVK DHLIHRCNRT
     LEHMFGYGLG EMLGRSIRIF YPDEAAFAEL SARLTPMLLE QHRFIDECEL VRQDGSRFWA
     RLSVQAIYPD QPEQGFFGMV QDITAEREAL EAMRQAKELA EQAAHAKADF LANMSHEIRT
     PMNAVIGMTY LLQKTSMTPQ QFDHLHKIQV SSQHLLGVIN DILDFSKIEA NRMSLEQVEF
     ELEPVLDNVV NLLAERAEKK SLELVLELAP EVPTRLVGDP LRLGQVLINF GNNAVKFTER
     GTVSLCVLQQ ERSDDTVLLR FEVRDTGIGI LPEQRDRLFQ SFQQADSSIT RKYGGSGLGL
     VISKRLAELM GGEVGVESVP GRGSTFWFTA RLKLGSGVPA RPALQLSLQD RRVLVVDDNE
     QAREVQAGML RFMGFDVTSA ESGPLALAEL ERSEQAGQPY DIVFLDWKMP EMDGLTVARE
     IARLPLSQQP RVLMVTAYDR DELVRAATEV PIHDVLVKPV TPSTLLDAVM RLLGTWQALP
     HSSLQGAAGG LDTSVLRGAS ALLVEDNEIN REVGQALLNE LGLQVELAPD GAVALEKVQQ
     RRYDVVLMDM QMPVMDGLTA TREIRKLSAL NDLPILAMTA NAMAGDRERC LEAGMQDHIA
     KPVDPNDLAV KLLKWVRPGP RSVLPADAAD AADAADAAEA DRAVELAASR LPGSSGETPV
     SLSLDGIVGL DAAQGLRQLQ GREALYLKLL RQFVSDQADM PARVAAAIAA GDWTQAERLA
     HTVKGVAAQI GAPSLRDLAE QLEQALQQRL PPAKIEPLRQ QLALSLPLLV SAIAARLSPV
     AVAAPAAFDP QRWQRLRERL ILLLEQDDTE CEILFESEEA LLRAGLGQRF EAVAQAIRDF
     DFPVALAAVR AAP
//
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