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
//