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Database: UniProt
Entry: A0A0Q5D8K3_9BURK
LinkDB: A0A0Q5D8K3_9BURK
Original site: A0A0Q5D8K3_9BURK 
ID   A0A0Q5D8K3_9BURK        Unreviewed;       684 AA.
AC   A0A0Q5D8K3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASF61_08845 {ECO:0000313|EMBL:KQQ36275.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ36275.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ36275.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ36275.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ36275.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ36275.1};
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:KQQ36275.1}.
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DR   EMBL; LMNW01000023; KQQ36275.1; -; Genomic_DNA.
DR   RefSeq; WP_056156503.1; NZ_LMNW01000023.1.
DR   AlphaFoldDB; A0A0Q5D8K3; -.
DR   STRING; 1736266.ASF61_08845; -.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; PF13188; PAS_8; 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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}.
FT   DOMAIN          305..523
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          568..684
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         617
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   684 AA;  73482 MW;  D4647E7223BEA733 CRC64;
     MIWNSAHGRP GFLDGGGEMG VLTRDHDWSA HPLGPPAGWS SLLKSTLRLV LASNHPMFIF
     WGDDLYQFYN DAYRRTLGAD RHPASLGQRG AECWNEAWHI IGPELAAVMA GGSPTWHENA
     LVPLTRNGKR EDRYWTYGYS PIEDEEGVRG VLVVCTDVTH DMRTRQLLKQ SYVTVVESMD
     EGLAVIRIML DDAGQPADYR FLEVNPAFER QTGLLDVVGK TARHLVPGLE ERWFQTYGKV
     ALTGESVRFL EGSAPMNRWF EVYATPVGPR DELMVALMFR DVSDRIRSEQ ALRTADRRKD
     EFLAMLAHEL RNPLAPISAA AELLQQPGTN AARVQHASAV IGRQVRHITG LIDDLLDVSR
     VTRGMIPLNT SATDLLRVVA DAIEQVRPLI DSHGHLLTVS TPPAPVLVTG DAKRLVQVLA
     NLLSNAVKYT PGGGDIMLRL DADGARVKLA VIDNGIGMTA DVLAHAFDLF VQAERETDRS
     QGGLGIGLAL VKSLVELHGG TVEAQSAGLG QGSRFTIVLP QLAAEAADGA AEDAPTAGGA
     AAAVAAEDGP AAASSGVPPA GAASHALRAM VVDDNEDAAA MLAMFLEIHG HAVLIEEEPA
     HVVQKALAFR PHVCLLDIGL PGMDGYELAR RLRATPELAG LVLIAVTGYG DAQARQQATA
     AGFDHHFVKP IDPAKLVALV ATLA
//
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