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Database: UniProt
Entry: A0A0Q5Z6B6_9BURK
LinkDB: A0A0Q5Z6B6_9BURK
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ID   A0A0Q5Z6B6_9BURK        Unreviewed;       667 AA.
AC   A0A0Q5Z6B6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASG30_18835 {ECO:0000313|EMBL:KQT13485.1};
OS   Ramlibacter sp. Leaf400.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT13485.1, ECO:0000313|Proteomes:UP000051173};
RN   [1] {ECO:0000313|EMBL:KQT13485.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13485.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT13485.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13485.1,
RC   ECO:0000313|Proteomes:UP000051173};
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:KQT13485.1}.
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DR   EMBL; LMQL01000003; KQT13485.1; -; Genomic_DNA.
DR   RefSeq; WP_055892442.1; NZ_LMQL01000003.1.
DR   AlphaFoldDB; A0A0Q5Z6B6; -.
DR   STRING; 1736365.ASG30_18835; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000051173; Unassembled WGS sequence.
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; 1.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KQT13485.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051173};
KW   Transferase {ECO:0000313|EMBL:KQT13485.1}.
FT   DOMAIN          17..133
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          145..215
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          289..506
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          536..653
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         65
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         585
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   667 AA;  72138 MW;  2DACE4917ABFDED8 CRC64;
     MDSASTIQST IDRGAHTVLV VDDNPATRYS TGRVIRAAGF KVAEAETGGE ALAMADKGVS
     AVVLDVHLPD MDGFDVCREL RSRPATELLP IVHLSAAYVK DEDHVTGLNA GADGYMVHPV
     EPAVLIATLQ ALIRARAAEE AQRRSERRFR AIYHQAHGGI ALIDAQGRFV DVNPAMLSML
     GRGREDVIGH GVASLAPQEF RERVEREFSG LAGEAWRGEF PLVNTDGAQV HMQWSLSASV
     GRDVRVATAI DVSERHELER RRHEVLEREQ AARAQAERHS RTKDDFIAVL SHELRTPLNA
     IIGWVHILKR RGATTEALKG LDAIERNVKT QARIISDILD VSRINSGKLQ LDRQWIDPAE
     LVTTSLASLS STLEERSVTV ETDVAGAHER AFIDAARYQQ ILWNLMTNAV KFSAQGGCVQ
     VRLARLGDNL RLEVRDYGVG IKPEFLPHLF DRFSQSDSPG NRRQGGLGLG LSIVKHLVDL
     HGGQVGAVSA GPGHGTLMWV DLPVGGAVDT GESIPGDLLG GEEEPEASAH ALDGVEVLLV
     EDDREAREMM AIVLGDRGAT VRVAADFDGA LEQLLQAPPH VIVSDIGLPG RDGYELARAV
     RAQEAGAARL PMIALTAFAR PEDQRKSLEA GFDRHLAKPL KPHLLLGAIV EMLPGAGTAG
     RPPGPQR
//
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