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Database: UniProt
Entry: Q021T1_SOLUE
LinkDB: Q021T1_SOLUE
Original site: Q021T1_SOLUE 
ID   Q021T1_SOLUE            Unreviewed;       690 AA.
AC   Q021T1;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, 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=Acid_3320 {ECO:0000313|EMBL:ABJ84294.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84294.1};
RN   [1] {ECO:0000313|EMBL:ABJ84294.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84294.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Janssen P.H., Kuske C.R., Richardson P.;
RT   "Complete sequence of Solibacter usitatus Ellin6076.";
RL   Submitted (OCT-2006) 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; CP000473; ABJ84294.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q021T1; -.
DR   STRING; 234267.Acid_3320; -.
DR   KEGG; sus:Acid_3320; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_0; -.
DR   InParanoid; Q021T1; -.
DR   OrthoDB; 9815750at2; -.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; 2.
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; 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; 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; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 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; 1.
DR   SMART; SM00091; PAS; 1.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABJ84294.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ABJ84294.1}.
FT   DOMAIN          37..93
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          110..162
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          334..546
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          567..683
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         618
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   690 AA;  77113 MW;  3134F015D43B49F5 CRC64;
     MPEPREELES QRVRELEELL TREIGARKRA EEALSQSEAR FRFIVKGFSE MVLAYDMDRR
     LTFVNAAAQS LTGYSAAELQ QEGFICWVHP DDRGRMLGYW DRLFTGLSFQ EEEYRLVTRD
     GRVKWMSASW GPLMDDNGRQ VGVQGREREV TERRMAEETL RIREQRYRTL FEESPFPMWE
     EDFSEVKRFL DALRARGIRE VGSHLMQNRE DLAECVRRIR ILDVNHAARQ FYGVSTKDEL
     MGDLSRILDE EGWDVICAEM ASLADGASMF KAEFETRTIL GEQRTVSMIV SLEPSPGDWS
     RVIVSFFDIT DRKRLEEQFL QSQKLESLGR LAGGIAHDFN NLLMVITGYS ELLLSDAGLS
     QRTMTGLREI RCAGDRGAEL TGQLLAFSRK QIGHPRALDL NALVRESQGM LERLLGEDVR
     LAVSLDPAAS AIRADRGQMH QVLMNLVVNA REAMPEGGTL WIETANVTEG GLGYVRLRVA
     DTGVGMDERT RLLVFEPFFT TKGASKGTGL GLATVFGVVT QAGGHISVTS EPGHGAVFNL
     YLPGVALPSN GDAALETKVK TSAGWGTLLV VEDQEDVRRL AVLILEGLGY TVLEAANGNE
     ALDVAREHQG CIRLMLTDVI MPGMNGRELA EQMTAIRPEM KVVFMSGYTD RIMSPDGVLD
     SSVHYLQKPF AAEQLNAKIR EVLDSGESVP
//
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