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
//