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Database: UniProt
Entry: A0A0Q8XGX2_9SPHN
LinkDB: A0A0Q8XGX2_9SPHN
Original site: A0A0Q8XGX2_9SPHN 
ID   A0A0Q8XGX2_9SPHN        Unreviewed;       504 AA.
AC   A0A0Q8XGX2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASE13_18110 {ECO:0000313|EMBL:KRC78240.1};
OS   Sphingomonas sp. Root241.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC78240.1, ECO:0000313|Proteomes:UP000051629};
RN   [1] {ECO:0000313|EMBL:KRC78240.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC78240.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC78240.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC78240.1,
RC   ECO:0000313|Proteomes:UP000051629};
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:KRC78240.1}.
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DR   EMBL; LMIV01000004; KRC78240.1; -; Genomic_DNA.
DR   RefSeq; WP_056619539.1; NZ_LMIV01000004.1.
DR   AlphaFoldDB; A0A0Q8XGX2; -.
DR   STRING; 1736501.ASE13_18110; -.
DR   OrthoDB; 9789238at2; -.
DR   Proteomes; UP000051629; 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; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.250.2580; -; 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; 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; 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   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KRC78240.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:KRC78240.1}.
FT   DOMAIN          1..71
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          73..125
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          126..196
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          194..253
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          273..490
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   504 AA;  54879 MW;  525BA021DA1BABA6 CRC64;
     MLAHFVASTE GRALFLADVD GSILTWNRGA ALLTGWDDDE IIGQPVTMLY PPADVAAKKP
     SADLGRAAAG QTVHEEAWRV RKGGSEYLAD VTTTCLRDVD GALCGYGLIL VDATERKAAE
     VALARSALHL RSILATVPDP MIVIDHRGVI LSFSAAAERL FGFSEADVIG SNVSMLMPSP
     DRDRHDTYLE RYLTTGERRV IGMGRIVVGR RRDGTDFPME LSVGDVQSDG HRIFTGFIRD
     LTEKQRAELR LQELQSELIH VSRLSAMGTM ASTLAHELNQ PLTAIANYLE ASRKLLERPE
     RNEAIESMFV EAIAESAKEA LRAGTIVRRL RDFVSRGDVE KHVEELPNLI DEASRLALIG
     ARERGIEANY ALDPKADAVL VDRVQIQQVL VNLVRNAVEA MSASPVRQIV IATKADRRGM
     VRISVADTGP GLAPEVDAQL FEAFTSTKER GMGLGLSICR TIVEAHGGRI WAEPRSGGGT
     IFNFTIMAAG GEEADDARTS HPPR
//
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