ID I3ZFF1_TERRK Unreviewed; 642 AA.
AC I3ZFF1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Terro_1666 {ECO:0000313|EMBL:AFL87969.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL87969.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL87969.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003379; AFL87969.1; -; Genomic_DNA.
DR RefSeq; WP_014785538.1; NC_018014.1.
DR AlphaFoldDB; I3ZFF1; -.
DR STRING; 926566.Terro_1666; -.
DR KEGG; trs:Terro_1666; -.
DR PATRIC; fig|926566.3.peg.1648; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_0; -.
DR OrthoDB; 100939at2; -.
DR Proteomes; UP000006056; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056}.
FT DOMAIN 229..281
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 282..324
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 423..637
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 642 AA; 70930 MW; 3A45F03133CB9629 CRC64;
MSMVVRVIAP SGRDAELILA LLRQNSIASE TCTDPLQLLT RGYDVGPMLI AEESLTSALI
AALAHFVNTQ PSWSDLPILI LTTVGRETER TRRLERERLP IGAPILLERP IRTATLLSSV
QAAVRARSRQ YQVRDAIAER DQNAARLRAE QETLRTVLDS MPVGVAVAHA NGEVVLTNAM
LAQILRHEEL PTPNFIAYSD WDTRHADGRK LTPEDYPLTR AIRSGRPVAG EDFLYHRGDG
TTAWIRLSAA PIVDAEGEIL GGVTAVIDVD QERKAAETLR RSEERFRLLI EQASVGIVIG
DLGGSLSYMN PTLLRALGYT HEEMEQGVIR WDELTPPEYA ELDLQAIKEL QTVGVAQPYQ
KVYVARDGRR IPLLLGAVRI PAQEKTDHEE IAVFLTDLSS QKQAEAALIQ SEKLAAVGRL
AASISHEINN PLEAVTNLLY LARSEQTTAA GREYIEQASQ ELARVSQIAG QTLRFHRQST
RPRSVTPREL IEPVLALYEG RLRNARVRAI SQHRGEPAFV CYEGDIRQVL NNLVGNAIDA
MRGDGTLRIR SRAATDQRTG QSGVRITIAD TGGGMSESTL QRIFEPFYTT KGIHGTGLGL
WISQGIVEKH HGLLRARSRE EGAHIGTVFT LFLPLEPGME DR
//
