ID A0A0Q5LJA6_9BURK Unreviewed; 890 AA.
AC A0A0Q5LJA6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF94_06125 {ECO:0000313|EMBL:KQR50382.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR50382.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR50382.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR50382.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR50382.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR50382.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:KQR50382.1}.
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DR EMBL; LMOV01000023; KQR50382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5LJA6; -.
DR STRING; 1736280.ASF94_06125; -.
DR Proteomes; UP000051403; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.3020; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KQR50382.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051403};
KW Transferase {ECO:0000313|EMBL:KQR50382.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 526..739
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 765..881
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 332..359
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 478..512
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 890 AA; 98567 MW; 02F7069438232310 CRC64;
MPYPSRSVLW TLLVLFGGMA ASMFLAGQLA WRHSLREESD TVERQLALYG QTLEQRIDRY
RTLPEVLALD DQLRSALTRP LARQEVERLN HKLERANGAS QSSTLTLLNA QGRAIAASNW
RTRTSNVGVD YSFRPYVQQA LAQGSGSFYG IGVTTGEPGY FLSQSIRDEQ GRTIGLVAIK
IALQELEREW LQTPDVVLAS DAHGVLFLAS QDAWRYRLLH PLDDDARAEL NATRQYADQP
LRPLDYRVIE RLDGGGQVVR MQAPDLPGRR LWHTRPLPGT PWQLHLLHEM HSTVADSRWA
AAAGAGGWLA LGLLVLFVRQ RQRLARLRLR SRQELETVLQ QHAQELRTAQ DGIVQAAQQA
AQQTDMGLSR SLEHLPQGVV IIDADLKLVA WNSRYVQLFR YPAYLMRVGQ PIEALLRHNA
RRGLLGPGPM QEAIERRLAH LRSGTPHLHE SAKDDGTVLE IRGNPLPEGG FVTSYADITS
YKNAARELRS LADALEQRVA DRTRDLEAAR QEAVRANRSK SRFVAAAVHD LLQPLNAARM
FTSLLRGHTL GEAERHAVDS IDGALASQDA ILSSLLDIAR MESGQLEVHV RDVALGPLLQ
VMGHNFGVLA EQRGLQLSCM PTRAVVRTDE NLLRRIVQNF VSNAIRYSRR GRIVVGCRRE
GDSHVRIEVH DQGPGIAESL QREIFEEFRR LDEGHADDRG AGLGLAIVER LGRLLGHEIG
LRSQLGRGSV FWVRVPLGDP TALRRIAPPP AATGQPADAP LHGSSAWVIE DDGPARAATQ
ALLQRWGCEV PLAAGAAQAL AQARPGQAPQ LVLLEVHLEA GRHGPEVYAE LCQRWGQTPA
VILVTAEGDA TLRRQAAERG WGFLARPVRA PALRALISQT LLRLQESQRT
//
