ID A0A0U5AZV6_9BACT Unreviewed; 837 AA.
AC A0A0U5AZV6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=THC_0904 {ECO:0000313|EMBL:BAU23289.1};
OS Caldimicrobium thiodismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23289.1, ECO:0000313|Proteomes:UP000068196};
RN [1] {ECO:0000313|EMBL:BAU23289.1, ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|EMBL:BAU23289.1,
RC ECO:0000313|Proteomes:UP000068196};
RX PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring, and emended description of the genus
RT Caldimicrobium.";
RL Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN [2] {ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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; AP014945; BAU23289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5AZV6; -.
DR STRING; 1653476.THC_0904; -.
DR KEGG; cthi:THC_0904; -.
DR PATRIC; fig|1653476.3.peg.938; -.
DR Proteomes; UP000068196; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAU23289.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000068196};
KW Transferase {ECO:0000313|EMBL:BAU23289.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..704
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 720..837
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 774
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 837 AA; 96519 MW; AD798E742D6AA2B7 CRC64;
MRDLKNFFFI LWILFLILFI QNVYAEPEEA LKTYTFGILA KRGEEVEKNR FYKLKEYLEK
NLPYKIQFLF LPFEELKKRA LKGEINFILT NPYQGITIKE LADKENIHFR IILSLGQYEK
GKYYPYFGGV IFTRKGSPIK SLSDIRGKVF GAVNPESFGG YLIALYELYK VGISEKEIRP
KFYGTHDAVV KAVLKGEVPV GTARTGVIER MISSGELSIK EIEILNQKVY PEFPLLISSP
LYPEWPILAL EGTPQKVIKD LARVLLEIEE KSSLAMATEA IFYLPFDYTP VNKLLLDLMK
GPYVELKEFY FQRFKEKYTP YFITLLLIFI IFLGLLAYGL FQRNRLLKTA KSDLEKEKAF
LDTVLKHTDF MVFYLSPEGH VIWANQKGQR ICLDEDNSTE PLWEICPYIN RMDRLKNLFE
KKELTKDYYN FVETIILEDV EKTFEGELIP LKKGQDLEGI LFFLRDISEK VIMEKQKIYL
EKLNVLKNVA GGLAHDFNNS LLGVINQIEL LKTKLNQKRL SREIKNLFEG IQDSLMSLRI
LGRELLTLVR GEAPVKEKVN FGDLIRDYTK LALAGKHGYE VFYEIESPLP AVEVDKELFS
ILWMNLVLNA IEAMPRGGRI FIKVKPKTKN GDTFLEVSIR DEGSGIEEKY LPYIFEPFFT
TKAGGSGLGL YVVKEVVKAH NGEIEVHSKV GEGTTFKIEL PTLKGELIPT FKPQKLTSKR
ILLMDDDDLI RDTLKELLQS FDYEVETAPD GESAIKFFTE ALREGKPFDY AIFDLIVPGK
LNGFETYQRI KELYPEVQAI LISGYFDEPV IHNYKAYGLK GALIKPFTIQ QLLELLE
//
