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
//