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Database: UniProt
Entry: G2E562_9GAMM
LinkDB: G2E562_9GAMM
Original site: G2E562_9GAMM 
ID   G2E562_9GAMM            Unreviewed;       739 AA.
AC   G2E562;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ThidrDRAFT_3425 {ECO:0000313|EMBL:EGV28986.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV28986.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV28986.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV28986.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) 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:EGV28986.1}.
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DR   EMBL; AFWT01000029; EGV28986.1; -; Genomic_DNA.
DR   RefSeq; WP_007042138.1; NZ_AFWT01000029.1.
DR   AlphaFoldDB; G2E562; -.
DR   STRING; 765913.ThidrDRAFT_3425; -.
DR   PATRIC; fig|765913.3.peg.3495; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG0745; Bacteria.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000004200; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EGV28986.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transferase {ECO:0000313|EMBL:EGV28986.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..109
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          306..451
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          453..598
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          621..737
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          130..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT   MOD_RES         670
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   739 AA;  79405 MW;  614AF810DE5160AD CRC64;
     MALDIKKFLG RFTGEARDHL ARLETGLATL SAGGTLDGES INGLFRAAHT IKGSARMLKL
     DSIADTAHQL EEVLGALRDG KLQQSSELGG LLMRAVDAIS ALVEQVEPTG GQLPSPDQAL
     CAALAQAAAG TSSTAETENP GVANPPDPEP DTPPSAPIAT SSACVRAPET VRVRMEKLDE
     LIKLMGEVVS SQAKFRQKLL EARALDAAFQ SLLSDTCAVS GVDATRLTEQ AAALHRFTLS
     LRDLIMEEEL LTGDLNDRAL IMRMLPLAIV FDPIARVSRE LGRDLGKEVH CEISGGEIEL
     DRHLIDRLSD VLVHLLRNAI DHGIESPQER QAAGKPSLGR IRLSARQEGV GILIEIEDDG
     RGLDRDKILA KAVQKGLIDS ASATLISDDQ VAELIFQPGF STSAIITDVS GRGVGMDVVK
     RTIVDDLQGA LSVSSRPGGG TLMRIQLPLS LAMMRILLFQ AGGQSFGLTA QHVAELIRIP
     SDETIQVADR PAVILRNEFL PLIPLAELLR LQESMGASDG AGSDRDTGGE SHLVVVIKVH
     QSTLGLVVDR LLDERDMVIK PLPEHLHGLG MVAGMVVTGT NELVSVLQAP ALLAAARRVR
     GETLTGTEPA RTIDEPPMGQ QILVVDDSRN TREIEKEILE AHGYRVTLAE DGLDGWQKAL
     GGHFDAIMTD VDMPNMDGFS LTARLRENDR YHGIPIVIVT SRQKEEDKQR GIQVGADAYI
     VKGDFNQSSL VETLHNLLG
//
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