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Database: UniProt
Entry: W4UN45_9BACE
LinkDB: W4UN45_9BACE
Original site: W4UN45_9BACE 
ID   W4UN45_9BACE            Unreviewed;       805 AA.
AC   W4UN45;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=JCM10512_96 {ECO:0000313|EMBL:GAE81929.1};
OS   Bacteroides reticulotermitis JCM 10512.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE81929.1, ECO:0000313|Proteomes:UP000019131};
RN   [1] {ECO:0000313|EMBL:GAE81929.1, ECO:0000313|Proteomes:UP000019131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE81929.1,
RC   ECO:0000313|Proteomes:UP000019131};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT   Isolated from the Gut of a Termite.";
RL   Genome Announc. 2:e00072-14(2014).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE81929.1}.
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DR   EMBL; BAIV01000001; GAE81929.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4UN45; -.
DR   STRING; 1445607.JCM10512_96; -.
DR   Proteomes; UP000019131; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00146; PKD; 1.
DR   CDD; cd17574; REC_OmpR; 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; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:GAE81929.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019131};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        227..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          282..505
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          550..665
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          699..799
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         598
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   805 AA;  91952 MW;  8CB437A6D7A242C9 CRC64;
     MAGTSNGLSK IDHQTQEITT YTKKDGLPSN MVCAIQGDDD GYLWISTNHG ISRFNPRDKE
     FINYFSSDGL QGNEFSRNAS IRSRDGKLIF GGLNGLVSFY PKEITKPVQD LKIRITDFYI
     YDEAVHKGSK SGPYEVVSQA VMNENFFHLS HEDNSFSIEF STMDFNNPER IIYSYSLNND
     KWVSLSPGSN RVSFNNLAPG TYHFKVKAQD YNNVSKEKEI TILISPAWYA SVWAKCIYAL
     LAIVIVYLFV QQVRQRYRAR QEMLEHIHGE QINEAKLQFF INISHEIRTP MSLIISPLEK
     LIRADNDSER QKTYSLIHRN ANRILQLINQ LMDIRKIDKG QMALKFQEAE LIGTLQEICT
     IFDYQAKNKQ IDFQFHHSID SLPIWIDPKS FDKIIVNILS NAFKFTPDNG KIDLYVNSDV
     EQESKRQWVE IMVSDSGIGI NEQERERIFE RFYQIRNSQN NSNIGTGIGL HLTRSLVELH
     HGTIEAVNNE DGKGCRFIIR LPLGNEHLLV EEIEDKATSP IPLSAAITLP IEESTSETEK
     EKTKNRRKYK ILVVEDDEEI RKYICDELGV NHYMTECTNG KEALTLILQK TPDLVISDVM
     MPEMDGITLC RKIKQNVNVN HVPVILLTAK SAEEDKLEGL SIGADAYISK PFSLEILKKT
     VVNIIQNREM LRNTYNGSQD QAENIPEMTL KSSDEKLMEK VMATIHSNIT NTQLNGEMIA
     KEVGISRVHL HRKLKELTNQ STRDLIRNTR LKQAASLLAS GKPIDVSEAA YATGFTNMPY
     FSSAFKELYG IPPKVYMEEH LKKTE
//
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