ID E0RT61_SPITD Unreviewed; 776 AA.
AC E0RT61;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=STHERM_c14170 {ECO:0000313|EMBL:ADN02357.1};
OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN02357.1, ECO:0000313|Proteomes:UP000001296};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 6192;
RA Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA Liebl W.;
RT "The genome sequence of Spirochaeta thermophila DSM6192.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADN02357.1, ECO:0000313|Proteomes:UP000001296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC {ECO:0000313|Proteomes:UP000001296};
RX PubMed=20935097; DOI=10.1128/JB.01023-10;
RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA Daniel R., Liebl W.;
RT "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT Spirochaeta thermophila DSM 6192.";
RL J. Bacteriol. 192:6492-6493(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; CP001698; ADN02357.1; -; Genomic_DNA.
DR AlphaFoldDB; E0RT61; -.
DR PaxDb; 665571-STHERM_c14170; -.
DR KEGG; sta:STHERM_c14170; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_104_15_12; -.
DR OMA; MDGWQFA; -.
DR Proteomes; UP000001296; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADN02357.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ADN02357.1}.
FT DOMAIN 1..68
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 136..357
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 372..493
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 522..636
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 677..770
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 426
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 571
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 716
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 776 AA; 87210 MW; D773F3F05DC5A05A CRC64;
MLLEVLEHVP VGMILLSPEG DILAANGRFF DMVDWTEEEL DGVRFPQIIY SSDEPVVSSF
IERLARGEVD QASILVRAAR KDGSIAWWRL WGFSRGGEVL LGAFDITDQK VTEEHLRKER
EEAIRSVQSK SRFLANMSHE IRTPLHTILG MTELLEDTRL DEEQRDYVQQ IRFSGEALLA
LINDILDYSK IEAGKLPMEI IEFDLYEVVE QAVGMVSLQA HKKHLEVVVD IGEEVPRKVK
GDPLRIRQIL VNLANNAVKF TEKGHVFCRV QLVQERKGVA WVAFTVEDTG IGIPENKKHR
LFRVFSQIDE STTRRFGGTG LGLAISKSLV EMMKGEIGVR SKEGEGSSFW FLLPLPIVES
YEPPVSLGEV GSLLLVEDYP LTRKVLHRYL QRYFPRIDEA STGAEALRKM RERAERGEIY
DLVLVDLTLP GMDGWQFASE VNADRSINDT RMVLMSPMGE GAEAKMKLLK WFDAYLAKPV
RKDDLYRTVA KVVNEEMELE AVEEAEGTEG GEETPADAGN YLILVAEDHI VNQELFLTIL
SRLGYRVELA GNGKEAVEKG LALKPDLIFM DVQMPEMNGY DAARVLREKG YEGPVIAVTA
SAFREDRERA LAAGMSDFLP KPFKKKDLLP VLQKWLSDTG KDRPAPESAS TRTAPAAEVG
GDDLFDLSGA REAFMDDLDV LSNVIDRFFE RLPQQFGRIE EALSSQDIET VRTEAHGIKG
GSWNLSMKLL GDLAAEMEAA AKEGDLSRCK QLFPRLKQGF VRTKEYVERS LSPQHS
//