ID A8F467_PSELT Unreviewed; 863 AA.
AC A8F467;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Tlet_0384 {ECO:0000313|EMBL:ABV32951.1};
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV32951.1, ECO:0000313|Proteomes:UP000002016};
RN [1] {ECO:0000313|EMBL:ABV32951.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV32951.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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};
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DR EMBL; CP000812; ABV32951.1; -; Genomic_DNA.
DR RefSeq; WP_012002432.1; NZ_BSDV01000001.1.
DR AlphaFoldDB; A8F467; -.
DR STRING; 416591.Tlet_0384; -.
DR KEGG; tle:Tlet_0384; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_322055_0_0_0; -.
DR Proteomes; UP000002016; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
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:ABV32951.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002016};
KW Transferase {ECO:0000313|EMBL:ABV32951.1}.
FT DOMAIN 516..560
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 653..860
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 259..286
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 863 AA; 99125 MW; 7A577D524B926AFF CRC64;
MSQIAQIICS QANAEHCDLF IYESQKDHFR LVGTTHQHEK IGVLKINSNT LMNDSHTIKL
EYNGKLTGAI ALRNPKNLPA IDNLLEELAF SLWWLDRFTE LENTAERYHN MSQLTDAFYS
YDDQDELKKE MVKVVAKILR ADMVLFLEKI SENYVFTAGF GIDRNQLLVE SIPQSHPFIS
KIEKSDSGIL NIKTQIDFAS IPVKSLIAVP LRLQDRILGV LIAINKISEE GYRTRYSFDE
FDLSTLHEVA RRISLAYTRL EYQNNLKKEI EKLKNYTKRY EDLIKQQQLY LKKMDLVHNI
SNAMRASYDP NNVYKILLLG LTSGRGLGFN RALLLLRDRK TETLFGKIWL GPSSEEDITK
IWREAERRAM SYGDFSQYLR EEALMLDISN GLTKKIEGKM FHYKDHPVFE RVVLRRKLIH
ITPPLAKSMG EAVKDLTNLL ETEEFAVVPL IGKWDTIGVL ILDNKFTGNP ISEIDTEVLK
IIADSAGLTI ENATNYEELR KKTESLEQQK NMIDYLRKFS ESILQNLTTA VIVIDRQGKV
LECNKRVEQL LGLPKERVIG SAYTDFGEAF QDVFGVAMKV FERGETITLS RYRIETANGE
RFFDTKYSPL WDIAGSSMNG VIVTLEDVTD QYLLEQERKD KEKLALLGEM SARVAHELRN
PITVIGGFLN RLKKNISDPQ ARERYLNILS NEVDNLQNIV SEILEFSRSA RNIDESKFQI
NELIEEVAFF MQEKAARNKI NLEFMLSPLQ EVVADRNRIK RVLINLVQNA IEATPQGGRI
ILKSQQDQDR VLVSVFNTGE PISEENLRKI FVPFYTTKTY GTGLGLPICK KIIEDEHGGR
IWAESKPEGT EFKFEIPIKR EGE
//
