ID E8T385_THEA1 Unreviewed; 384 AA.
AC E8T385;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Theam_1253 {ECO:0000313|EMBL:ADU97217.1};
OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Thermovibrio.
OX NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU97217.1, ECO:0000313|Proteomes:UP000006362};
RN [1] {ECO:0000313|EMBL:ADU97217.1, ECO:0000313|Proteomes:UP000006362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15698 / JCM 12110 / HB-1
RC {ECO:0000313|Proteomes:UP000006362};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL Submitted (JAN-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};
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DR EMBL; CP002444; ADU97217.1; -; Genomic_DNA.
DR RefSeq; WP_013538003.1; NC_014926.1.
DR AlphaFoldDB; E8T385; -.
DR STRING; 648996.Theam_1253; -.
DR KEGG; tam:Theam_1253; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_0; -.
DR Proteomes; UP000006362; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 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 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 PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADU97217.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ADU97217.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..94
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 167..383
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 384 AA; 44405 MW; FC5D3DD6F2C8CFC4 CRC64;
MEGVLTALVI FLVLLFSVAT LAFLYERRKR RELLNQMRRL RRELRRREPP VDRSKLLARA
LSLIREGIVI MDPYGRIVFT NRFARELLDI KPEDTGKFFY QAIKNFDIVS LINEAFNEKY
KVWQEKKVKD RYVQIIFGSD MDEKVLLLID LTPIKQYENL KKDFIANASH ELKTPLAALK
LSLEALEEEC GNNPKASHFV KRALERITFM EQLIEDFLTL SRLDSTNLTV KLQEVELLPL
VREILKGLSD FIVRKQLKVK LSVPQEAAVY ADEKMLYAVL KNLIDNAIKY NRDGGEIEIS
FREHAKEVEI SVCDTGYGIP KSHLPFIFER FYRVERSRSR KLGGTGLGLS IVKLAVDKMG
GKVEVETREG EGTCFRVYLP KRGV
//
