ID G2E204_9GAMM Unreviewed; 1147 AA.
AC G2E204;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ThidrDRAFT_2317 {ECO:0000313|EMBL:EGV30953.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV30953.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV30953.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV30953.1,
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:EGV30953.1}.
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DR EMBL; AFWT01000015; EGV30953.1; -; Genomic_DNA.
DR RefSeq; WP_007041030.1; NZ_AFWT01000015.1.
DR AlphaFoldDB; G2E204; -.
DR STRING; 765913.ThidrDRAFT_2317; -.
DR PATRIC; fig|765913.3.peg.2356; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000004200; 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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
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; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 4.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS51371; CBS; 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGV30953.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 13..68
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 76..137
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 141..197
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 207..270
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 296..366
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 370..422
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 634..855
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 888..1004
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1047..1142
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 937
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1086
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1147 AA; 126127 MW; 99FA067B108413DA CRC64;
MLSVTDLTLA DIMNRRIRHV PPDCPLEEAA SQMAVSRISS LLVLEDGHPV GIMTERDLLR
FSHQHRDPRT PVSELMTSPV ITLSEKISFP DAYRTALAQR VRHLIAVDDA GDLVGVATET
DFRRHLGFSF LRRLDDLTDA MDRDLPLLSP EAPLDDALAL MMQRRTSYAL AADGRLARGI
LTERDIPRLL ASGMLYTGRQ LLLHEVMQAP VQVIAHHTSV TETARLMQDL QVRHLAVVDE
DGLLIGMVTL HRLMERISAI LLQNHAWYQV DRPSNDTPLA EHGLQLASEV SEILATEDRL
QAILDAVPDL VWLKDPNGIY LACNPAFERL FGAPRAAIIG RTDYEFVDRE LADFFRTNDL
QALKSSGPRL NEEWLTFATD GYRGLFETAK TPMFDTSGRL IGVLGIARDI TERKQAAEAL
DRHRNGLEAL VHSRTNELEA ANRALRKNDR RLEVLFELRQ LAFDLNEEAL LQRGVEAAVE
ISESRIGYLC FVEEDQERIG LCVWSSGAER LCSVGHEIPD AVSGVGLWAD AVRDRRPVLH
NDCREIPDQG GYPLGQCDLI RHLVVPVLEG GKVRLLVGVG NKPNDYEASD VRQLRLFAED
LWRIRMRRRA EIALAEAKEA AEVANQAKSA FLANMSHEIR TPMNAIIGLA HLLEREVTAG
NPRAHVAKIK EAANHLLDVI NDILDFSKIE ADQLVLERSR FVPERLIEDA CALVADRANA
KGLRLLRRVA PEVPQALWGD SLRLRQILLN FISNAVKFSD SGEILVEIRA EKVSEQRCWI
RLSVRDEGIG LTDDQRERLF HAFVQADDST TRRFGGTGLG LAICKRLASL MGGDIGVDSE
VGRGSTFWVC LPFDLANETP VGEPSVSGSD GSVPPSDLIL ARRHAGARIL LVEDDFINQE
VALALLKNTA LVVDVADNGE QALAKVREEN YALVLMDMQM PVMDGLSATR AIRRLPDRAD
LPILAMTANA FDEDRQQCLA AGMNDHIGKP VEPERLYAAL LRWLPSGSGR TDAASASKTP
ATPPASLDGV VIAGLDTARG LASVAGNQTI YLKLLGRFVA NHGDDAAKLR QTLVAGDPAE
ARLLAHTLKG VAATLGAEAV RQRAAEIELA LREGAAPAVI DSGIMNLERD LLGLIEALAN
VGLALNA
//
