ID D0MGR5_RHOM4 Unreviewed; 857 AA.
AC D0MGR5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rmar_2758 {ECO:0000313|EMBL:ACY49628.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY49628.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY49628.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
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; CP001807; ACY49628.1; -; Genomic_DNA.
DR RefSeq; WP_012845238.1; NC_013501.1.
DR AlphaFoldDB; D0MGR5; -.
DR STRING; 518766.Rmar_2758; -.
DR KEGG; rmr:Rmar_2758; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_15_10; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000002221; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
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; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACY49628.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002221};
KW Transferase {ECO:0000313|EMBL:ACY49628.1}.
FT DOMAIN 83..156
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 159..211
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 233..282
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 337..408
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 412..462
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 480..699
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 729..850
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 453..480
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 535..562
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 782
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 857 AA; 97718 MW; 8A5F3C8EE42EFA6B CRC64;
MEAVSITCWT PTAEAPLPAE LAERLPPEAR RWIETLRENP PQAPLAHPFD TATGPLLLLA
LPYPSDPPLL VVALDLRTIF PETDTFFRTL VQSLRAVLWE ADARTFRFTY VSPQAEELLG
YPVHRWLEEP DFWTAHIHPE DRDRAVAYCR ETTDRGEDHD FTYRMICADG RVVWVRDIVT
VVPDEQGRPH RLRGLLLDIT EEQETRRELE VFRQRYQDLI SNNPIATGVY CRGQVVYANP
AMARLFGAER PEDLLGKTAT DLIHPSNLEA ALENARKVVE RREPVSYGRG RIQRLDGRSA
IVDFRGVPIT WEGARAVLFF MWDVSEQLRT ARRLAEREAQ YQALFENAPA PMYVRRDRQF
LLVNPAFVRL TGYTAEELTA PGFDAMRLIA PQSIPVVQER LARRRQGLPV PPRYELWIRR
KDGKEILVEA ISINIRWEGE PAVLGFFRDL SAQHEAETYL QQARRQAEEA SQLKSRFLEL
MTHEIRTPIS TILGYADLLR DELADRIPPE LLEFIDVIRE SGRRLLGTLS DVLDLSLLET
QRRRLETEAV NLNELARRLE TDFAPMARAK GLRWETEVPE QPVRVVADEE ALHRALANIV
HNAVKFTESG TVQLRVGQHG GEGWIQVRDT GPGMDPAFAR TGLFEPFRQE SEGTNRHHEG
AGLGMTVARR FVEAMRGRIE VDTAPGRGTT VTVHLPLLEA QPSPTASALH PEAPDLRRLQ
QRLRAHHPRI LIVEDNPENA RFLELALQDV AEVTVAADAT RALEAIDAHL LENRRFDLIL
LDLNLPGDFN GQALLHEIRR RPAYHHVPVV AQTAYAEPFR PEDFLAEGFD GFLIKPIDRL
TLYRELDRLL TRQPTPS
//
