ID K4LHF8_THEPS Unreviewed; 282 AA.
AC K4LHF8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Tph_c22460 {ECO:0000313|EMBL:AFV12436.1};
OS Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermacetogenium.
OX NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV12436.1, ECO:0000313|Proteomes:UP000000467};
RN [1] {ECO:0000313|EMBL:AFV12436.1, ECO:0000313|Proteomes:UP000000467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC {ECO:0000313|Proteomes:UP000000467};
RX PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA Schink B.;
RT "Genome-guided analysis of physiological and morphological traits of the
RT fermentative acetate oxidizer Thermacetogenium phaeum.";
RL BMC Genomics 13:723-723(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003732; AFV12436.1; -; Genomic_DNA.
DR RefSeq; WP_015051308.1; NZ_KI912609.1.
DR AlphaFoldDB; K4LHF8; -.
DR STRING; 1089553.Tph_c22460; -.
DR KEGG; tpz:Tph_c22460; -.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_020211_8_0_9; -.
DR OrthoDB; 1677679at2; -.
DR Proteomes; UP000000467; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR032834; NatK_C.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR039506; SPOB_a.
DR PANTHER; PTHR40448; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR40448:SF1; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF14501; HATPase_c_5; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFV12436.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000467};
KW Transferase {ECO:0000313|EMBL:AFV12436.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 154..281
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 282 AA; 31879 MW; 82D972D7E7029273 CRC64;
MKKGSLVLVP LLLGVGIVLL AVDFYLFWSI QFDRPLTRGA IYIIDSTILS LVLVLLFICW
KVYRFEKSEL SRALNSLYSE HLQELLRVVR LLRHDFANHV QVISALLQTN QIEKAKAYIT
SLGQRIQIPK GMLQFGIPEL GALLMVKMHV ADLKNISFDI EVDTDLKSLK VDPLDLNTII
GNLLDNAFEA VESGEEEQKR VVLRFFETPE SYFIQTINPG YLDEEMREKI FSPGFSTKQG
SNRGFGLVSA KTAVEKYGGR INVACSQREG VKFTVMFPKM VA
//