ID E0RQM5_SPITD Unreviewed; 1272 AA.
AC E0RQM5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=STHERM_c05640 {ECO:0000313|EMBL:ADN01529.1};
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:ADN01529.1, 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:ADN01529.1, 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; ADN01529.1; -; Genomic_DNA.
DR AlphaFoldDB; E0RQM5; -.
DR PaxDb; 665571-STHERM_c05640; -.
DR KEGG; sta:STHERM_c05640; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_006625_0_0_12; -.
DR Proteomes; UP000001296; Chromosome.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 4.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 4.
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; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 381..453
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 460..511
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 606..658
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 655..710
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 728..780
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 798..1020
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1044..1160
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 499..533
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 768..798
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1093
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1272 AA; 144284 MW; C54952DB24FF6197 CRC64;
MTSSRGGGEI SSLEESLEEV SLDMGAPGAS LCLTITYELQ EIARWEAPDA VTLLDALLLS
TDEGRFWIEG FELRNFTHLS ILDGRIHLYP LKVGGFLYGI LAVDSPSHPE AFLSHKSRYE
QAWFSALPWE RIFTPGFRLD IAKNLLPSLR TGLLYLDVRT RSIDLHLPGS STSPSTSLTL
SEPEFLATVE PDARKSLEEF LAAPHDTFHG RFSFPGRGRT SFLVIPLPVQ GRILPFLLLD
VHAETLYFES LQEQRRLFTS VLDSFTDYIL VTDSDRRILY ANTAFETWAY LLEGRPLPSL
VGKPISLVSR AIDAHLRPLL EEAEKSDTVI LREISWQHRA EEITTEVTIF PLHKDYETAR
WLIILHNITH RKRTERLLSQ QKQFYRQMLE ALPIGVYTLD PLSDYTVSLW NPYMERITGV
PRQKALGVPE TRLFPPPLSE ELEVLNRKIL EDPLTRVLVP SMEVEFPHQE ESRIVKVQKR
GVLTPEGELD HILVLLEDIT EQRRTEEELE RYRNHLEEEV ARKSAELARA AMEMDAILRS
TESVAICSMD RDLRIQIFNP TLARLSRMYF KRPPRREMRF TDLFPTRTMQ RQVETAVSRV
LSGQTFTTRF SVSRRNLLPL HLEVVISPKR NEGGEILGAT VIAMDITQRA TVERQMRLFK
AIADTAPYGT VIIDANHTIV YANPYMARIH GYRLEEVMGQ HLSIFHTEEQ YEKLIEELTR
AEDVGVMPSQ EIWHVYQGQL PFPMLTTATF IKDEEGHVTY IGIVSLDMSL QKEAEQKLKE
AKEEAERAMR AKSEFLANMS HEIRTPLNAI IGFTDLLASS FPSGKEASYL DAIRSSGKNL
LMLINDILDL SKIEAGKMTL SYSPVDLRSF IEEIANIFRT QVEHKGLSFI LDYAPALPPT
VEIDELRLRQ VLFNLIGNAI KFTEQGHVKV QVRGSLHTEE SKVDLTISVE DTGIGIRPEE
REAIFQSFHQ SSGQDTRKYG GTGLGLTISK RLVEMMGGTI SVESEYGKGT TFTVNIPDLT
CSTERMVSAT EETGGDVPMY EGKVILVVDD KDLNRTLLKE YLAPTGATVI EASNGQEALS
RAEAHPPDLI LMDIRMPVMD GLSFIKEYYR DPSHRNIPVI ALTASVLKER HEEFLRNGFV
EVLTKPIQKD ALFSTLRSFL PTETSRTAAP PPPREEHLEF TAEDLARRAQ ILSLYDREIA
PLLEEAKETW LNTTLEELGS RAKEAGTRIG SPFLSGWGAS LEEAVQSFNI HRIRTLIKEF
EEKIGRLKEE SL
//
