ID A0A0Q7DG50_9BURK Unreviewed; 1330 AA.
AC A0A0Q7DG50;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC67_06440 {ECO:0000313|EMBL:KQW70110.1};
OS Methylibium sp. Root1272.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1736441 {ECO:0000313|EMBL:KQW70110.1, ECO:0000313|Proteomes:UP000053968};
RN [1] {ECO:0000313|EMBL:KQW70110.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW70110.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW70110.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW70110.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KQW70110.1}.
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DR EMBL; LMDY01000012; KQW70110.1; -; Genomic_DNA.
DR STRING; 1736441.ASC67_06440; -.
DR Proteomes; UP000053968; Unassembled WGS sequence.
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; cd19410; HK9-like_sensor; 1.
DR CDD; cd00088; HPT; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR007891; CHASE3.
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; IPR013767; PAS_fold.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 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; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..472
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 481..531
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 687..911
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1071..1193
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1229..1326
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1120
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1268
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1330 AA; 144650 MW; 9E0B8EDA81FF25F9 CRC64;
MSLTATALFI AAGRPASFGL RNLSTGLGLS AAALALVALL QDEFGWQLAM HELSFGSSTS
VEQPLHSGQE TPRYGQLGYG CLGLTIAGLS RSRFVPLVWL AAFTTTLLGV AAVTVRVWKT
SNIDADLAID RISVATLLSI MLLGLGSLIA FARRDRHDAL APAPTRMSIE FKVFGGLVGA
VVLMAVGGGI TYRTSARFVD SAEQVAHTQE VRARLGEMYA SMSDAESSQR NYLLTGAVGQ
RLVSSAHAEK ARSKMLTLQS QLADNPSQTE RLAALAMVME HRLQDLDRIA DLRDRDGLEA
ARAAVSENTG NVLVSRYLAL TSEMDAIEAV LLSQREARAA RERRDYLAFL MLTLAGATAI
FVMMLTGVRR EMLARREADD AVRALNTDLE RRVEERTAAL VANQRRFVDL FECAPAALVM
TDNRGAIVQV NRQTEIIFGW DRTALIGSQG DMLMPEQDRE GFAMLRDAYL SEPRPQAMGK
TRPDLRGLRR DGSIFPVDVS LNPLNTGAEL MVLAAIHDTT ERGRMTEALR ASAALYQHTL
DSMLEGCQIF DFEWRYLYIN STAERQNRQA REGMLGRTVM EVSPGFEHSE VFAAMRRCME
QRSPQQLEHE FLFPDGSRVW FHVSILAALE GIAMFSVDIA DRKETEEEIR TANAELERRV
ADRTSELVLA REAAEAANRA KSAFLATMSH EIRTPMNGVI GMVEVLSHSN LPDLQADAVK
TIRDSAFSLL NIIDDILDFS KIEAGRLELE RSTASLSDLT EAACDALLPM ADDKGVGLDL
DISPDLPEQI WTDPTRLRQV LLNLVGNAIK FSGGRPHQPG LVSIRVDTEV GDPQRLVLEV
RDNGIGMTAE TIAQLFSSFN QAEASTTRRF GGTGLGLAIC QRLVILMGGS IAVQSRMGQG
SVFTVHLPLE AVEGQRLRSQ PDLRGVDCLV IGGAQATTFE RYLVHAGASV QTPPTLAAAV
TQAGGLARPV LIQDCRRSGQ AADVFSATCA VLPDARQVLV TRGRGRRARL SFGNAVTLEG
DCLRRVALLH AVAIASARAS PDEVYETDFD EPGVIRMEPP SIAEARAQGR LILVAEDDEI
NQKVILRQIE LLGHTAELAN DSVEALRLWR AGQYGLLLTD LHMPGMDGYS LAMAIRAEES
KRGTAWRPRM PILALTANAL KGEAVRALAA GMDEYLTKPL LLRALRSAIR RWLPGEAEDS
MPVPLEEPGV TTAGLVVDVE VLQSLVGNDQ AVVREFLLEF RNSARALAAE LSVARADDDI
RRIGSIAHRL RASSRSVGAI ALGDLCAELQ NACRTGKRES VALSLVQFDT ALSAVDHRIG
ELLVASPVAP
//
