ID A0A0Q7EFJ8_9CAUL Unreviewed; 799 AA.
AC A0A0Q7EFJ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC65_08135 {ECO:0000313|EMBL:KQW82238.1};
OS Brevundimonas sp. Root1279.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW82238.1, ECO:0000313|Proteomes:UP000050923};
RN [1] {ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW82238.1, ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|EMBL:KQW82238.1,
RC ECO:0000313|Proteomes:UP000050923};
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 -!- 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:KQW82238.1}.
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DR EMBL; LMEB01000006; KQW82238.1; -; Genomic_DNA.
DR RefSeq; WP_056451545.1; NZ_LMEB01000006.1.
DR AlphaFoldDB; A0A0Q7EFJ8; -.
DR STRING; 1736443.ASC65_08135; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000050923; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 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; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000050923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 233..285
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 286..356
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 360..412
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 430..647
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 667..784
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 716
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 799 AA; 85591 MW; 3623A31ABDD73644 CRC64;
MARSKTSKTL NLDSPFERLT ALARAMFGTP HAMISVVAGD RTLFKASTRL GVTELPRGVS
VTRLVTAEGA DAVLVIEDAL EDPRVCDHPM VVGEPHLRFF AGASVSNAAG EAVGAIGVMD
VNPRPRLNEA EIENLRVLAR MAGDIVERAE ANRIQAEKLE LLRLAEEMAG VGQWRLDATS
MLVTWSDEVY RIHGVERTAF DPSCDDAIGH YHPDDQGPLR AAVMHALATG QGYKLRLRII
RPDGAERLVL AQADTDRDET GRVLSLFGVF QDVTDQEMAA RRVADSERRY RLLADRATDI
IITYGMDQRV LYVSPAIEAI IGHTPDEVVG RDVTDLIHPE DVPGLMEGVV AFVRGDATQR
SMTYRVITRS GDIRWMEART TLVRDAAGQA LEFQDVVRDI TATKRLEQEL TEARDRAEVG
ARAKSEFLAN MSHELRTPLT SVIGFSGLLQ SSAALPEAER RYADRIGTAS EALLGVINDI
LDYSKLEAEA VSLEPRAFDP RAMVEAAATM VEGQCAAKGL RLAVTLDPTA PAVLTGDEGR
LRQVTLNFLS NAVKFTASGA VRVAMGWNGA SLRVAVSDTG IGIAPDKLAA VFERFTQADA
STTRVYGGTG LGLAISHRLI EMMGGQVGAE SRPGEGSTFW FEVPLGAAEA LDQAAAAGEA
PSPEGLRILM ADDAAPNREL VAAILGGMGV TLHAVADGAQ AVEAARTGGY DLILMDVHMP
VMDGLDATRA IRALEGEARR TPIIALTANV QPEQIERCRA AGMDDHVGKP IEVGQLLRVI
AARLADQDAA GSDAAVAVA
//
