ID H5WR26_9BURK Unreviewed; 1099 AA.
AC H5WR26;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BurJ1DRAFT_4536 {ECO:0000313|EMBL:EHR73324.1};
OS Burkholderiales bacterium JOSHI_001.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR73324.1, ECO:0000313|Proteomes:UP000004674};
RN [1] {ECO:0000313|EMBL:EHR73324.1, ECO:0000313|Proteomes:UP000004674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR73324.1,
RC ECO:0000313|Proteomes:UP000004674};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA Woyke T.;
RT "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL Submitted (NOV-2011) 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; CM001438; EHR73324.1; -; Genomic_DNA.
DR AlphaFoldDB; H5WR26; -.
DR STRING; 864051.BurJ1DRAFT_4536; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_302447_0_0_4; -.
DR BioCyc; BBAC864051:G1H30-4516-MONOMER; -.
DR Proteomes; UP000004674; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EHR73324.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004674};
KW Transferase {ECO:0000313|EMBL:EHR73324.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..329
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 655..707
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 725..944
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 966..1087
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 698..725
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1020
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1099 AA; 119480 MW; E35499AF766B6B37 CRC64;
MPMAETAPPT QQPLPFDRQA QRGVRERILR YFFGSAAAIS ALAALLFWLL ATYIPPLPRL
AVGAWFGGIS VASLAALRLR PALLQRSMLG VALAAVAGIG LATAAAGTGI DSPSISFLGL
ITCMVCASST RRIGTVVALA CGALLCGLAL GEWRGALAGG GGQVVPLSMR LAMEVLAVVA
GLVGGVLMER ITLSHVGAAV EREQRFRSLL AIAADAYWET DEQLELRHAW RRSRSAGQFV
PLELPDGHLA WALPTLQMES NALKQVREQM QARRAFREVP AQRQLPGGRL VHLLTSGEPR
FAADGQFIGY WGLVRDVTQE VLAREALAET ETRYRELFDQ VPIALLVHRE GRVQAANPAA
ARLLGFANPS AMVGADLLAS FATDGNRDSA LARLQARPDL LLPGMDPGDP QAAFTLQART
LGGRALLLNA TGVPVDTPQG LATLSMLLDQ TEQHIAEAAT RRWQTLLERL VLASPDAITL
TDLETGRYEM VNAAFLRLTG WDSTQQVVGH TSFELNIWQN ADERQQLLGG LAKSEVVQDL
RISFRSRHGD AVPVRLSATR FLMDGREYLV TNSREIDSSE RARLEREAIL DNASIGIALT
RRQRFMLANR RFEQMLGWPP GALVGQHGRV AWPSDDEYAE VGRTVGPMLA RGEQVEVERR
LQRQDGSHFL ARILAKAIDP TRPADSGTIW TMEDVTERRA TEAALARARD QAEAANRAKS
AFLANTSHEI RTPLNGLVGL AKLARAPELD ETRRRQYLDQ ISESAQALSA IISDILDLSK
IEAGKLELET VPFDLHELLQ GLHRAYSALA DARGLHCTLQ TELGLPEHVR GDPLRVRQIL
SNFLSNALKF TPAGGIRIVA QAPDDQGFVR FEVHDSGPGI DPGVQARLFQ PFSQADDSTT
RRYGGTGLGL SICRELAQMM GGEVGADSLP GEGSCFWVRL PLPEADMQGA DSGFAGLDAN
PLQGARVLMV EDNAVNMMIG VAMLEQWGAQ VRQASDGGQA VEEVLRAARG ERPFDIVLMD
LQMPGMGGHE ATRMLRRYFD RRALPIVALT AAALVSEREA SMQAGMDGFV TKPIDEKRLH
DTLVRVLAQR KLAELDPPT
//
