ID A0A0Q5LYJ1_9BURK Unreviewed; 684 AA.
AC A0A0Q5LYJ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF94_07645 {ECO:0000313|EMBL:KQR50322.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR50322.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR50322.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR50322.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR50322.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR50322.1,
RC ECO:0000313|Proteomes:UP000051403};
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:KQR50322.1}.
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DR EMBL; LMOV01000023; KQR50322.1; -; Genomic_DNA.
DR RefSeq; WP_056667050.1; NZ_LMOV01000023.1.
DR AlphaFoldDB; A0A0Q5LYJ1; -.
DR STRING; 1736280.ASF94_07645; -.
DR OrthoDB; 8807260at2; -.
DR Proteomes; UP000051403; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051403};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..681
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 684 AA; 74879 MW; D3C4CE317B5169CF CRC64;
MHKHSRKLTF RWIAGTLWRP PHVWLLFALM LLAQGGCVAA SGSHAEGIGV VGARLSVERV
DDPGHALTPD EVAALHDGHV VPNMQLPLSA GYLDRTVWLR FHSPGGESSV QPSLWLLARP
TYVDSVTLYQ RAAGAHGSWQ VQASGDLVPG HEKAGVRQPL FELQPHALTL VRIRTTSAMQ
FDAQLLTQAQ LRQTLVEDER QQGLFFGMLF ALLASIVGAT AIFRTPQLCA LAVLCAVGTL
HIFNLHGYLS LWVPSGLTRR ASDAVGMGAF GLTTALAWQI RLQLTSELQH RAVRKLLSAV
ASAAALGMAS PLLGLYGSVA WTNLVLIGLC DLIAIALCWA NLRRNPRSAV NGVLLAAYVV
HALSGILPAL GLLGWVRMEV DATLIWQTEI FVFMLLATCA VFAEMVVRYR DATEARAVAL
RHLAQSEQIL EQRVKQRTAD LLQAQFALAQ ALDSERVLRQ EQHHFFQMIS HEFRTPLTVI
DSAASEQLRF PTHALENQTE RAAQIRRACR RLTSLVDSCL ITDRMDASGF HILPSSVSIT
ELLEHAAQLV RWSPRHQLRL STRAAPESWV CDATLVRIAL SNLVDNAVKH AKDGEIVVTA
AQNPAGQLEI SVADEGHGIS PQSIQKIFDQ FERGHRADQT RGFGLGLWVA RRVARLHGGD
ILVTSQIGQG TRFTMSIASQ LPVG
//
