ID A0A0Q5V926_9CAUL Unreviewed; 539 AA.
AC A0A0Q5V926;
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=ASG17_02585 {ECO:0000313|EMBL:KQS57617.1};
OS Brevundimonas sp. Leaf363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS57617.1, ECO:0000313|Proteomes:UP000051182};
RN [1] {ECO:0000313|EMBL:KQS57617.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS57617.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS57617.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS57617.1,
RC ECO:0000313|Proteomes:UP000051182};
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:KQS57617.1}.
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DR EMBL; LMPZ01000001; KQS57617.1; -; Genomic_DNA.
DR RefSeq; WP_056098652.1; NZ_LMPZ01000001.1.
DR AlphaFoldDB; A0A0Q5V926; -.
DR STRING; 1736353.ASG17_02585; -.
DR OrthoDB; 9805942at2; -.
DR Proteomes; UP000051182; 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 InterPro; IPR025919; Stimulus_sens_dom.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13755; Sensor_TM1; 1.
DR Pfam; PF13756; Stimulus_sens_1; 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:KQS57617.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051182};
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 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..303
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 311..536
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 539 AA; 58352 MW; 86BD66256DFA4B63 CRC64;
MASDTATARA DRPADETAPR RFERFRFGGS RLGGLILALN LVSLLILFGG ALALNEWSRG
LIQARQQSLA VQAALLANLL GEFGATSGDP YPALNPENAS ILLRDNFIPS DQRARLFDID
GHMLTDSYAV TDEIPGRGLP AAHPAGTPVA PQSTPETQRR IDRAHVELAG EIERALDGQP
QSSVRRNENG DRVVSVSIPV RHVQQVLGVL TLETGDVDAI LGAQRRALLP FAFVALAVSL
LSSLLLHLFI ARPVKRLSAA ADAVRLQQAR AISLPELEGR KDEIGDLARS LETMTETLSD
RMDAIEAFAA DVSHEIKNPL TSIRSALETL SLVKTDAQRD RLTALLQQDV RRLDRLITDI
SNASRLDAEL SRDRPRAVNL ATLLTEIVGV YRAGAKPGEA EVQLSLPQGD AAPVMGRDGP
LGQVVRNLID NARSFSPPKG KVRVALFRED ADPLPIRIRI EDDGPGIPPD NLETVFERFY
TSRPKGAAFG TNSGLGLSIV RQIVEAHGGR VWAINRTSAD DQIQGARFEI ALPSVGRRP
//