ID A0A0Q7DWA8_9CAUL Unreviewed; 545 AA.
AC A0A0Q7DWA8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC65_11330 {ECO:0000313|EMBL:KQW81871.1};
OS Brevundimonas sp. Root1279.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW81871.1, 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:KQW81871.1, ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|EMBL:KQW81871.1,
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:KQW81871.1}.
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DR EMBL; LMEB01000007; KQW81871.1; -; Genomic_DNA.
DR RefSeq; WP_056453131.1; NZ_LMEB01000007.1.
DR AlphaFoldDB; A0A0Q7DWA8; -.
DR STRING; 1736443.ASC65_11330; -.
DR OrthoDB; 9805942at2; -.
DR Proteomes; UP000050923; 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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR025908; Sensor_TM1.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13755; Sensor_TM1; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQW81871.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 250..305
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 313..539
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 59470 MW; 2FDA1B7109D935AA CRC64;
MALDTVTARA EPADDDRPRR VRRFGGSRLG GLILALNLLS LLILFVGALL LNEWRRGLIE
ARQETLTAQG ELLVQVLGEE QIGVTRGAPT PYLDSIEASR WLRDNFIPAG QRARLFDVDG
IPVADSYEVT EAIPGEPLPP ALPAGTPPRA VDPEADKEDA EQLDKAHAAL AAEVEAALDG
VQQAGVRLSE NGDRVVSVSI PVRHVEQVLG VLTLEAGDVD ETLAAQRRAL MPFALVALFV
SLLSSLLLHL FVARPVMRLS AAADEVRLQR SRAISLPDLE GRKDEIGDLA RSLETMTETL
SDRMDAIERF AADVSHEIKN PLTSIRSALE TLPLVKTDEQ RERLTALLQN DVRRLDRLIT
DISNASRLDA ELNRERPRII DLTVLLNEIV GVYEAGIKPD GAHVTFSSEA LEHAFVRGRD
GPLGQVFRNL IDNARSFSAP GGTVKVSLFR DELDFDRPVH VRVEDAGPGI PAENLETVFE
RFYTSRPKGA AFGGNSGLGL SIVRQIVEAH GGRVWAQNMQ RADGEITGAR FEVALPAVIP
VSRRP
//
