ID G2E7M8_9GAMM Unreviewed; 1356 AA.
AC G2E7M8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ThidrDRAFT_4291 {ECO:0000313|EMBL:EGV27912.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV27912.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV27912.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV27912.1,
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:EGV27912.1}.
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DR EMBL; AFWT01000053; EGV27912.1; -; Genomic_DNA.
DR STRING; 765913.ThidrDRAFT_4291; -.
DR PATRIC; fig|765913.3.peg.4365; -.
DR eggNOG; COG0715; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000004200; Unassembled WGS sequence.
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; cd01007; PBP2_BvgS_HisK_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 6.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR InterPro; IPR015168; SsuA/THI5.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF09084; NMT1; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 1.
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; SSF53850; Periplasmic binding protein-like II; 3.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EGV27912.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:EGV27912.1}.
FT DOMAIN 868..916
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1015..1236
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1243..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 851..878
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1248..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 151145 MW; D84D8B30D052CD45 CRC64;
MAFSRRPSPR GMADLTALLV LLLSLTPLRG MARDAPSADP LTRVSVQLTW KHQFQFAGFY
AAIAQGFYRD RGLSVELREY TQGLDMLDEV RSGRATYGIA NGSVIDWRLA GEPVVLLANY
FRKAPLVVLG QPGIRTLNDL RGKRLMAEET ELRSPLLSAA LRETGLVPGT NLTIRPHAFD
AGPFIRGEVE ATTAFFTNEP FELERKGIPF QTIELNGYLP GLGDDYLFTS ETQASTHPER
TRAFVQASNA GWRYALDHPD EIVELILDRH SRRKSHEALA YEADKTRDLI LPFSAPIGAL
LPRRIEMVAS ALLDAGHPGS LANLQGFLFD EGTPIRAPHR PPNPLDYSGA ERAWIKAHPR
VSLRVDADDA PYSFVDGTGT LDGILVDLVR AMCEDAGLEP NLTPGSHAKM DQESREPGIQ
GYLNFDYHDA GASGSFLGIE SPIPPMYALY TRRPNEFSSD GLRNLKGKRI LLAKGMDPTE
QGFSAADNQY QWVETPEEAF ERLLSDRADA YFANFAHVQW HLHRHFITDL TPLYFSSGYP
DPMLAVFKEY PELHAILKKA YGHVSNRLPS LLARWQLEQA GASRPALTKE QRRWLSAHPV
IRYAVNPNWA PIESLDRDGH PTGMAHEYIQ RIQDLLGVRF EPVAVASWTD LRERFEHGEI
DVLPGIVETQ SRRAHYRFTA PYLTFPVAIF APAGAPFLGS LDALADKKVA VVGDYATHEW
LRQDHPEIVT VPVATTAAAL KEVAEGRVDA FVDNLVTTSH AIGQDGLLEI RMAGTTPYEL
SVGMAVRKDW PVLVDILEHA IAALPKIERD GIYNRWVQAL PPAVVDYGLL WKALAVCALV
LAVTLYWNRR LRREMRMRRH AEQTLADSER RYREMVESAG TSDFHFYSIT PSGLIGYVTP
GSFKLFGNAS ETILGRHWRE VVTWPEPAIE LFESAIGICL NGQVPEPVTL EFSRNGVRQQ
LISHPRPVKD ERGRTVRIEG IAVNLTARLQ LEEQLFAAIT AAREANQAKS IFLATISHEI
RTPMNAIVGM IHLCLDSPLN AEQHGYLQAA RRASESLMQL LNGILDESKA EAGRLTLEAR
PFALRELIEN LNALVARRGQ GSELAFRYQI DPEIPPRLLG DPLRLGQILT NLIDNAVKFT
ERGEILLSVR MPEIQERRLR LEFTVRDTGI GIDEAEIGNL FEPFRQADSS ITRRYGGSGL
GLAISRHLVE LMGGTIDVTS RIDEGSTFRF DIWLDRPAAP NEALTAHRVP KDVPRVPEEE
TERQGGPDTA LPMTPKTLAA TASGGSSPET VLTELRERAE RRDPTTEDVL AEHRQVLADA
LSPESFRMLS DQIENYRFGE AAVTLDDLVR TFEISK
//
