ID D1CJ30_THET1 Unreviewed; 593 AA.
AC D1CJ30;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Tter_2868 {ECO:0000313|EMBL:ACZ43750.1};
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Chloroflexota; Thermobaculum.
OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ43750.1, ECO:0000313|Proteomes:UP000000323};
RN [1] {ECO:0000313|EMBL:ACZ43750.1, ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX PubMed=21304745;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL Stand. Genomic Sci. 3:153-162(2010).
RN [2] {ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(2010).
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; CP001826; ACZ43750.1; -; Genomic_DNA.
DR RefSeq; WP_012876780.1; NC_013526.1.
DR AlphaFoldDB; D1CJ30; -.
DR STRING; 525904.Tter_2868; -.
DR KEGG; ttr:Tter_2868; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_0; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000000323; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; 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; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003660; HAMP_dom.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR031967; PhoR_single_Cache-like_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF16736; sCache_like; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACZ43750.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACZ43750.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..242
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 247..295
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 313..370
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 374..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 593 AA; 65043 MW; 6D21BCD3B21D452A CRC64;
MFTRIQWRIA ASYVLLIAVA LLALGVYLAY YLRQEQLHQL EMDLRSQALI IAQQVAPQLQ
RGDASQIDAF AKRVGRAADV RITIIDRTGR VLGDTDHDPN TMDNHLSRPE VRQALASGFG
ESMRHSRTLD RDLLYVAVPI GSGGDTLGVA RVAMPTSDVQ ASLNRVVTVV GAATAIAIVL
AILLALVVAR ATTSNIARLT SAARSMAAGQ LHQRIEIDGR DETSELASAF NEMAQSLDSY
ISTINRERER MSAVLSYMAD SLLITNARGE VQAMNRAAEQ LLDVREQDVR GRSVMAVIRD
HELAGLVRRA LEMQGPVRLP RLLELGSDGN RRLIDALASP IPGENGTGSQ VLLLLRDVTE
LRRAETIRQE FVANVSHELR TPVAALKSLV ETLEEGALED EEVARDFLAR MHVEVDKLAQ
LIEELLELSR IESGKVELRI HPVNLVEVVR AGAERLRPQA ERQGVDLEVT VEQPEILALA
DPERIQQVVI NLVHNAIKFT PPGGRITVRV YSLDREVAVT VQDTGVGIEP ELLDRLFERF
FKVDRARSAG GTGLGLAIAK HLVLAHRGRI WAESEGMGKG ARFTFTLPAV GAA
//
