ID W4UNV1_9BACE Unreviewed; 1460 AA.
AC W4UNV1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JCM10512_514 {ECO:0000313|EMBL:GAE82318.1};
OS Bacteroides reticulotermitis JCM 10512.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE82318.1, ECO:0000313|Proteomes:UP000019131};
RN [1] {ECO:0000313|EMBL:GAE82318.1, ECO:0000313|Proteomes:UP000019131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE82318.1,
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:GAE82318.1}.
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DR EMBL; BAIV01000003; GAE82318.1; -; Genomic_DNA.
DR RefSeq; WP_044159936.1; NZ_BAIV01000003.1.
DR STRING; 1445607.JCM10512_514; -.
DR OrthoDB; 1108380at2; -.
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; 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; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; 2.
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; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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:GAE82318.1};
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 Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1460
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004849779"
FT TRANSMEM 880..905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 927..1143
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1194..1309
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1352..1451
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1242
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1460 AA; 167088 MW; 966FA796D37163CB CRC64;
MKPLLCLLFV LSTTLSSFAQ PYCKVDHFSV NNGLSQGVVA NIIQDQKGFM WFSTWNGLNK
FDGYTFKNYK AFPGDKSTLT TNRFSYIAES KYGDIWCLTY DGRAYLFDNQ SKEFIDILHP
IEGSLQQTPP VTKIYTLKKG IAWIVCEQGY TFRVDEKACK QGEGITLYST FNKSLKGEKI
LNIYQDADGD EWILTDKGIN IVGKKQINSD FPFKLMQEYD GKIYLVTTSG KIASYKPATK
DIKFIQIPHP INEINSIASI SAKNDSICMA TDNGLLLYLP QKNQFQLFDI RTSPKLSNNV
VSFYRDRTGD VWLFSEDPGV IRLNLQTGEK QVLLSPPQDI VHYEVKSRIL IFEDKEGTLW
VVPQEGHLCY YDRKSQQLKL YFTDPHNPTS LFAPYIRFFF PDRQGNVWLI TTRGVEKMSF
SPHVYELNNI DNGLEIRAFL LDKQRQLWVG SKRGIVRIYH ADGTLKGYLT PQGTITPQET
KFSRSVYCFL EDKEGNIWLG TKKDGLLLLK KKNDQSYSVQ QYLHDPDDAY SLSDNSIYSI
FQDSHGRIWL GSYGKGINLI SRNEDNKIQF IHCGNQLKNY PVNSSLKIRY ITEVRNGILM
VGTTHGLLTF SAKFDQPEEI KFYHNVRDPE AATSLGSNDV TYIYTDSSQR IYVTTFTGGI
NQVVSSNLLS DNIVFKSYTI RDGLASDLVL SMIEDGQKKL WVVSENALSI FDPVKGSFDN
FISKHIANEL NFSEAIPSLD NKQRLLFGTD HGVLKINPSQ MKKSSYVTPI VFTDLKIQGS
QRRVAIDDVK ELTLEPSERN VTFQFAAIDY ANPEDIRYSY RLKGLEKEWN DADKNRSATY
INLPPGEYQL QICSTNSDGA WTDNLRTLDI KVLPTFWETY WAWIFYVLLF ALFTSAIVYI
LFYIYRLRHQ VDVEQQLSNI KLRFFTDISH ELRTPLTLIS SPLAEVLDRE PLSPTAKGHL
LLVHKNTERM LRLVNQILDF RKIQNKKMKV LAEQIEIVSL VDKIMENFRM IAEEKDISFE
LQAAQDSLYV WADKDKFEKI LFNLLSNAFK YTPAGKSVTV HVKTIEDKLQ IVVSDEGIGI
DRDKQKSLFQ RFETLGRYNI LQPSSGIGLS LVRELIELHH GSIEINSEPG VGSEFIVNLP
LDKKVLEEDK QVEFILTDSI TNTLAEQTAA PQNLYEDEDG MEQEAALNDE EAFSILIVED
NQELRTFLKN ILSENYIVLE ATNGEEGAEI AQEQIPDLIV SDIMMPVMNG LDMVKAIKEN
NDTCHIPIIL LSAKSSLDDR IAGLEQGIDD YITKPFSSTY LRTRITSLLK QRKQLQEMYL
AQLAGKKVEE SDNYEAEPAR PQITPYDELF MQQVMEFMEE QMDNTDLTVD DFADKLMLSR
TVFYRKLKSI VGLTPVDFIR DIRIKRSIQL IESGEYNFSQ VAYMIGFSDP KYFSKCFKKQ
TGLTPSEYKD QAQLSTHSTG
//
