ID A0A0Q5DFF1_9BURK Unreviewed; 980 AA.
AC A0A0Q5DFF1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF61_05280 {ECO:0000313|EMBL:KQQ40195.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ40195.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ40195.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ40195.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ40195.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ40195.1};
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:KQQ40195.1}.
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DR EMBL; LMNW01000012; KQQ40195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5DFF1; -.
DR STRING; 1736266.ASF61_05280; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 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; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 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; SM00065; GAF; 1.
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; SSF55781; GAF domain-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; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 532..584
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 595..823
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 851..973
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 906
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 980 AA; 106523 MW; 09300EBF466B66C6 CRC64;
MSTINPAVSA FAPDADFLAL FDAVPSPCLA VTPALVIVAV NDAHLRATGA RREQLLGRRL
FDAFPDNPAL DRPDGAANIG AAIARVLDTR MPDTLPVQRY DVPAEDGIGF VERYWKPVHV
PVLGADGAVR YVIQHAEDVT QRVRDANQAA SMRSELVAQA QTIRDQHSMA ELFRQAPVFM
AMLEGPCHRY TYVNAGYRQL LDGRPVPGLT VAQALPEAQQ QGFIALLDQV YRTGTAHTAN
GVRCLVTAPA GSATTERHVD FIYQPVRGAD DAVTGILVHG TDVTDRVLRE LRRHALVRLG
DAARRVRHPE DILMQACVIL GETLGVSRVG YGSVDALAQT FTVAREWSAP GARLPPATLR
FGDYGTFFEE LRQGRLVAID DVDFDPRTRD VAAALKARNA GALVDVPVIE QGELVALIFV
HSAQPRSWSD EDVALIREMA ERARATSERL RSDIALRASE ASLRTIANAM PQMVWSTLPD
GLHDYFNQRW YDFTGMPVGA TDGDAWNGLL HADDQPRAWS VWQHCLASGD TYEIQYRLRH
VSGRYHWVLA RALPIRDDAG HIIRWMGTCT DIHEQKLAEA EWRQASQRKD DFLAMLAHEL
RNPLAPISTA AQLLKLRGSR EPGIEHASDI IIRQVRHMTD LVDDLLDVSR VTRGLVQLEQ
HELELMAIVH GAVEQARPLL EARRHALVLR LPPDQLFVRG DRTRLVQALA NLLNNAAKYT
PQGGEVVLAL DVRRDHADRH GAANAEAVLS VTDNGIGMPP ELLPRVFDLF AQAERTPDRA
QGGLGLGLAL VKSIAVLHGG SAVAASDGAG KGSTFTIVLP LLSPAVLAVA APAALPLAHL
APSAASARQR RLVVVDDNQD AGRTLGALLE ALGHQVAIFN DAESALRASA AWEADGAAAA
DAFILDIGLP DMDGYELARR LRARPATADK LLIALTGYGQ AHDRVLSRAA GFDHHFVKPV
DHAALGRLLA DPTVVSGNDR
//
