GenomeNet

Database: UniProt
Entry: A0A0Q8QAD8_9SPHN
LinkDB: A0A0Q8QAD8_9SPHN
Original site: A0A0Q8QAD8_9SPHN 
ID   A0A0Q8QAD8_9SPHN        Unreviewed;       560 AA.
AC   A0A0Q8QAD8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASE00_17020 {ECO:0000313|EMBL:KRB80961.1};
OS   Sphingomonas sp. Root710.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB80961.1, ECO:0000313|Proteomes:UP000051854};
RN   [1] {ECO:0000313|EMBL:KRB80961.1, ECO:0000313|Proteomes:UP000051854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root710 {ECO:0000313|EMBL:KRB80961.1,
RC   ECO:0000313|Proteomes:UP000051854};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB80961.1, ECO:0000313|Proteomes:UP000051854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root710 {ECO:0000313|EMBL:KRB80961.1,
RC   ECO:0000313|Proteomes:UP000051854};
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:KRB80961.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMIB01000016; KRB80961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8QAD8; -.
DR   STRING; 1736594.ASE00_17020; -.
DR   Proteomes; UP000051854; 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   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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 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; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KRB80961.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW   Transferase {ECO:0000313|EMBL:KRB80961.1}.
FT   DOMAIN          139..191
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          192..263
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          338..555
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   560 AA;  62108 MW;  53552086E0DE8B8D CRC64;
     MEALWRRLRE EGRLHTEVIE RHRDGDELVI HDHAKLFDHG NGRVSAVIAV TDVTEWRKAE
     AALRLSEARL ATAVSVQGIF IYEIDLLAGR TIWTTRSEAF FGRPLVDPDP ASPETMDSEH
     YLQISKVIET VKRTGEDRCH FDFTFHYPDG SERLAEGWAR IIRDGAGRPV RMLGTHLDVT
     ERRQREQALR DGEAERRAIL ATVPDAIFVC TERGIVRACS ATACELFGYA EEELVGRNML
     DLFQDGRSLA ALRRDLKAAI KQGPDARWPL PMNVRRADGT LVPTSFVIGD AMVEGTRMYV
     VCGRDMRPTI ATEERFHRLS NDLAQVSRLG MMGEMAGALA HELSQPLSAI VNFLGAADLM
     LEGGAAADSE RLRNAIHRAS EQSTRAGEII RRLRAFILRG EADMRAEHVT SLIREAAALA
     LFNTSSFGVR LAYDFESEER LVLGDRIQIQ QVLVNLIRNA ADAMAAHGGA RRELLIQTMM
     ARDNLIEIAV RDSGPGIAPE MLERLFSPFA TTKREGLGFG LAISRRIVEA HGGQLSAAAA
     PDGGAVFRFT LPVMEEEGPR
//
DBGET integrated database retrieval system