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Database: UniProt
Entry: A0A0R0DRC2_9GAMM
LinkDB: A0A0R0DRC2_9GAMM
Original site: A0A0R0DRC2_9GAMM 
ID   A0A0R0DRC2_9GAMM        Unreviewed;       418 AA.
AC   A0A0R0DRC2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ABB34_08860 {ECO:0000313|EMBL:KRG84671.1};
OS   Stenotrophomonas daejeonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG84671.1, ECO:0000313|Proteomes:UP000050940};
RN   [1] {ECO:0000313|EMBL:KRG84671.1, ECO:0000313|Proteomes:UP000050940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG84671.1,
RC   ECO:0000313|Proteomes:UP000050940};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-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:KRG84671.1}.
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DR   EMBL; LDJP01000050; KRG84671.1; -; Genomic_DNA.
DR   RefSeq; WP_057640952.1; NZ_LDJP01000050.1.
DR   AlphaFoldDB; A0A0R0DRC2; -.
DR   STRING; 659018.ABB34_08860; -.
DR   PATRIC; fig|659018.3.peg.1789; -.
DR   OrthoDB; 2514702at2; -.
DR   Proteomes; UP000050940; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220:SF9; HISTIDINE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KRG84671.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050940};
KW   Transferase {ECO:0000313|EMBL:KRG84671.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          308..408
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          184..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  45214 MW;  31294D5E7A1363CF CRC64;
     MIASLWFCLR ILVAWVLALI VLGVLWSNLF GGPGAVFVLL VVGLLVLAAI NTASHLRRVK
     LVAGRLDHDS LSSRQQRRIE LPLDAGQAFA LVESVVAGLP RVMDIESSPG SLQVRARIAR
     ADSYNTRPPS RWNPLAWLAV KRDRVSATVT PGEGTSSVAL LFEPDAGAWV DLLLADEGSN
     RENADAMSRA LGQRVAEQRR DERESAARTE AEKELSVARL NLLHAQVEPH FLYNTLANAQ
     VLTRTDPERA ERMLGHLIQY LRSSLPGIDQ SLSTLGQELE RVQAYLEILR IRMGERLAVQ
     VDVPEALRDV ALPSMALQTL VENAIKHGLE PKSGGGTIWL LAREADGQVH ITVADDGRGF
     GGSSSGTGIG LKNLRERLRL TCGPEAAFAL VSNFPSGAAA TLTLPHKGAL PPELPHAS
//
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