ID A1AW26_RUTMC Unreviewed; 720 AA.
AC A1AW26;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rmag_0361 {ECO:0000313|EMBL:ABL02133.1};
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthturnera.
OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL02133.1, ECO:0000313|Proteomes:UP000002587};
RN [1] {ECO:0000313|EMBL:ABL02133.1, ECO:0000313|Proteomes:UP000002587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm {ECO:0000313|EMBL:ABL02133.1};
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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; CP000488; ABL02133.1; -; Genomic_DNA.
DR RefSeq; WP_011737758.1; NC_008610.1.
DR AlphaFoldDB; A1AW26; -.
DR STRING; 413404.Rmag_0361; -.
DR KEGG; rma:Rmag_0361; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_019564_0_0_6; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000002587; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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 InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABL02133.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..370
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 506..720
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 720 AA; 81841 MW; B096825F1743FDCE CRC64;
MIFSQYLSLK KTPPAWVWVF VFLLSISGTF YLGLNPDFIE HWWGYLVGFN IIMSFVAIYY
VYADVLRLKR DVKGGIVGSK FTWSFVKIVP VLVIVPVLSF YIFSFQTIQN NVKDSEKAFN
VFSQNFIQQV NGLYSGVQKI RDERYTEQTK RLLTLITSFG SFQKDAENYA QSMQIFLDGL
IDKGWACQIT LLNAQEEVVA KTADVTNCMA IEEQPLPGTQ PRMINEDETA NVIQVKMSTR
YLSNISNQDL FVVDMVYATD PGLLGFLSQV RGFANAAQNI KFEINTSITQ KRFMIDFSST
VLLAILSALM VVFRMIERLM KPLNNLSIAT KEIAKGNYDV RITKQKESED VRSLIEQFNT
MSRQIKASRE GLDTHNLYLE TILKYSYGVI ALDQNRKIRL INPVIGTMLG IEDEKLFFGK
KCSTIVDRYS NLEPLFLMTQ DKFKRDESEW SEEIKITLAN QHLLLSCQGA ALKNDNETLG
FVIVIKDISR LNRTQKKAAW GEVAKLMAHE IKNPLTPILL SAQRLRNRFM DSLEGKDLDV
IDKTTNTIIH QVQSMDTMVS AFADYANTPQ IERKPCDLNM LIKQSIALYD SQSNMNIDFD
LFAGIPLLLL DSHSISRVLI NLVKNASEAM IDGRDLNVKI ITEYLPKQAI VRLNTIDDGD
GFDKYVLDRV FEPYVTTKIK GSGLGMAIVQ NIIKQHEGKI FASNVKPHGA MITIEFNCNK
//
