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Database: UniProt
Entry: A0A0Q5HTJ7_9BURK
LinkDB: A0A0Q5HTJ7_9BURK
Original site: A0A0Q5HTJ7_9BURK 
ID   A0A0Q5HTJ7_9BURK        Unreviewed;       763 AA.
AC   A0A0Q5HTJ7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASF77_05020 {ECO:0000313|EMBL:KQQ97316.1};
OS   Massilia sp. Leaf139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ97316.1, ECO:0000313|Proteomes:UP000051760};
RN   [1] {ECO:0000313|EMBL:KQQ97316.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ97316.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ97316.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ97316.1,
RC   ECO:0000313|Proteomes:UP000051760};
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:KQQ97316.1}.
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DR   EMBL; LMOJ01000001; KQQ97316.1; -; Genomic_DNA.
DR   RefSeq; WP_056335286.1; NZ_LMOJ01000001.1.
DR   AlphaFoldDB; A0A0Q5HTJ7; -.
DR   STRING; 1736272.ASF77_05020; -.
DR   OrthoDB; 9808408at2; -.
DR   Proteomes; UP000051760; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQQ97316.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        303..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          323..376
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          406..459
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          540..761
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          361..391
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   763 AA;  81954 MW;  1BAC35E1BFFCCEA0 CRC64;
     MRIGLRSLLP RGLRARLALA FSLLSVILTL ALLGLVERRA VGRLENQIGE GLADLAFQTS
     DKLERGMFER YREVELIAGR IAPGDAAQDA ARMAAMLRRV QDSYAYYEWI GMVGVDGKVK
     AAGNGLLVGV DVSRRDWFRQ GLEGGFVGDV HDAVLLAKLL PPQSEPRRFV DVAFPYADAE
     GRVQGVLGAH LSWNWARDVE RSVVGSAART SPVQALILNG EGRVLLGPPD LADKVLALES
     LRRARTARRG GHLVEAWPDG RTYVVGYQQG SGHGNYPGLG WTVLVRQDVS QAYAPVRDMR
     AQVLWSGAAL ALLFSIVGVW VARSITRPLA RLAGAATRLR QGGIETIDAR ADDYAEVRAL
     GRALNALVTD LEARREQLER LNGSLEQVVE ARTVELRRAL AGVQASEARI RAIVETAQDA
     FIGVDMTGRI LDWNRQAELL LGWRREEAVG QILSDLILPA ELRAAAGGAL ADFAGGARRR
     LDHLNQRVER VVTDRHGAEI PVEMSTGLTG EGDSAVFSIF LRDITERKRI EAMKNEFVGT
     VSHELRTPLT SIRASLALLA DGALGALPPD VLELIEISNN NCMRLNRLVD DMLDIQKIEA
     GMMSFAPVLQ PLLPLAREAV RTMRGMAGAA GVCLVLEGET AGEGPTAAFD YDRMTQVLVN
     LLSNAIRVAP GGTQVVLRVA ADGEGANLAV ADSGPGIAPA LRERVFQPFV QIGDAGSAPK
     GGTGLGLAIC KRIVEEHGGT ITIGDAPGGG ALFCVRLPAR MPA
//
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