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Database: UniProt
Entry: A0A0Q7AFW5_9BURK
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Original site: A0A0Q7AFW5_9BURK 
ID   A0A0Q7AFW5_9BURK        Unreviewed;       757 AA.
AC   A0A0Q7AFW5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASC76_08905 {ECO:0000313|EMBL:KQW39174.1};
OS   Rhizobacter sp. Root404.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW39174.1, ECO:0000313|Proteomes:UP000051611};
RN   [1] {ECO:0000313|EMBL:KQW39174.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW39174.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW39174.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW39174.1,
RC   ECO:0000313|Proteomes:UP000051611};
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:KQW39174.1}.
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DR   EMBL; LMDS01000004; KQW39174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7AFW5; -.
DR   STRING; 1736528.ASC76_08905; -.
DR   Proteomes; UP000051611; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16919; HATPase_CckA-like; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd18161; REC_hyHK_blue-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; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43065:SF46; C4-DICARBOXYLATE TRANSPORT SENSOR PROTEIN DCTB; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
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); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KQW39174.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051611};
KW   Transferase {ECO:0000313|EMBL:KQW39174.1}.
FT   DOMAIN          1..20
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          94..146
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          138..214
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          273..327
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          389..614
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          637..752
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         687
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   757 AA;  83286 MW;  1DFC8B754F41F0E9 CRC64;
     MAGVVQDVTE RRRVLRELEQ SERRFRALAQ AMPNQAWLAQ PDGLLDWFND QVYAYSGAPP
     GGLDGHRWSE MVFSADLPQA QARWAASLAS GEPYEVEFRL RRADGEYRWH LARAIPVRGE
     DDRVIHWIGT NTDIHEQKTA EVEHALERNR LWSMSQDLLL VCDFEGRITA INPSSQRMLG
     WTEDDMVGHL LADFIHPDDL RSSLDEVGKL AQGETTLAFE NRYRAKDGSY RLLDWTAVPD
     AGRIHAVGRD ITDERAIALN QERIWTLSPV LKIVAAADGR LSTANPAWIQ VLGWSLAQTE
     GRMLLDFVVT DAVSAVREAL VRLAAGERVV EQQFAMNASD GGARQIVWTI VGESGVLYGF
     GRDVTEQRAA EDALRQSQKM EAVGQLTGGI AHDFNNLLQG ITGSLDLVQK RIAQGRLDEL
     DRFVRGAVGS AKRAAALTHR LLAFSRRQPL DPRAVRANPL VASMEDLLRR TLGERIELEL
     VLAGGLWLTR CDPNQLESAI LNLAINARDA MPDGGRLVIE TCNAHLDSAY AARQRDVRPG
     QYVCICVTDT GTGMSADTVA KAFEPFFTTK PIGQGTGLGL SMIYGFARQS EGYAKIYSEV
     GHGTTFKLYL PRHRGEAPDD EPLAELTEAH VTLHGETVLV VEDEAVVRGL IVEVLGDLGY
     RAIEAADGPA GLELLQSRAR IDLLITDIGL PGLNGRQIAE AGRQVRPGLK VLFMTGYAEN
     AAIASGFLEP GMSMITKPFA MEALATRIRE IIEAPPD
//
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