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Database: UniProt
Entry: A0A1C7H786_9BACE
LinkDB: A0A1C7H786_9BACE
Original site: A0A1C7H786_9BACE 
ID   A0A1C7H786_9BACE        Unreviewed;      1524 AA.
AC   A0A1C7H786;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A4V03_02155 {ECO:0000313|EMBL:ANU59630.1};
OS   Bacteroides caecimuris.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1796613 {ECO:0000313|EMBL:ANU59630.1, ECO:0000313|Proteomes:UP000092631};
RN   [1] {ECO:0000313|Proteomes:UP000092631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I48 {ECO:0000313|Proteomes:UP000092631};
RA   Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA   McCoy K.D., Macpherson A.J.;
RT   "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT   Diverse Mouse Microbiota 2 (sDMDMm2).";
RL   Submitted (APR-2016) 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; CP015401; ANU59630.1; -; Genomic_DNA.
DR   RefSeq; WP_065540242.1; NZ_NHMU01000002.1.
DR   GeneID; 82185932; -.
DR   KEGG; bcae:A4V03_02155; -.
DR   Proteomes; UP000092631; Chromosome.
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; 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; 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; 4.
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; 3.
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};
KW   Kinase {ECO:0000313|EMBL:ANU59630.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000092631};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:ANU59630.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1524
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008887109"
FT   TRANSMEM        912..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          958..1175
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1236..1351
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1422..1521
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   REGION          1392..1415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1284
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1524 AA;  174493 MW;  1330B7C42D14C283 CRC64;
     MMKKTLISII LLLAIAFSTY AQQHCFFTHY STEDGLSQNT VMNILQDHKD NLWFATWDGI
     NRFNGYTFKT YKARQRNYIS LTNNRVDRMY EDRYGFLWLL TYDNRVHRFD PKTETFEQVP
     AAGEEGSAFN VHTIEVMPNG TVWLLTENDG AIRILTHPDE NNRLTWDIYS SKTELFPSLH
     VFKVHQDKAG NDWLLTDNGL GIIRPGKKEP NSYFTETKGK FGGMNQAFYA VQERDKDICF
     ASDHGRIWSY QKESGEFTLI ELPTKGQITS IHPIAPDVSV ITTDSDGFFT YNLRTKTNVH
     YSFLTCKALP AKPILSAYVD RSSEVWFEQE EPGVVAHFNP STGVVTREQI PIEYSNPERS
     RPAFHIHEDV NGYLWVHPYG GGFSYFDPQK KCLVPFYNGL GSRDWRFSNK IHSAFSDKQG
     NLWLCTHSKG LEKVTYRNVP FTMIIPMPHE HESLHNEVRA LCEDKLGNLW VGLKDGILRI
     YDADKTYKGY LTENGTISAT GTPMPGTVYH VIQDSKGIIW IATKGDGLVR AEPTSSNGMS
     YKLTRYLHRE DDMYSLSDNN VYCIYEDHYG RIWLATFAGG INYITKNEAG KTLFINHRNN
     LKGYPIDPCY KARFITSDNN GRLWVGTTTG AVAFDENFKK PEDVKFYHFS RMPNDTQSLS
     NNDVHWIIST KKKELYLATF GGGLNKLVSI SKNGHGEFKS YCVLDGLPSD VLLSIREDSK
     QNLWISTENG ICKFIPSEER FESYDERSIT FPVRFSEAAS ALTAKGSMLF GASGGVFIFN
     PDSIRKSSYI PPIVFSKLTV ANEDITPGGN SLLKVDIDDA DKLVLSHKEN IFSVHFAALD
     YTNPQNIQYA YILDGFEKQW TFADKQRSVT YTNLPKGEYV LRVRSTNSDG VWVDNERILD
     IVILPSFWET PIAYVLYILF ILIIILVAVY ILFTIYRLKH EVSVEQQISD IKLRFFTNIS
     HELRTPLTLI AGPVEQVLKN DKLPADAREQ LVVVERNTSR MLRLVNQILD FRKIQNKKMK
     MQVQRVDIVP FVRKVMDNFE AVAEEHRIDF LFQTEKEHLY LWVDADKLEK IVFNLLSNAF
     KYTPNGKMIT MFIREDENTV SIGVQDQGIG IAENKKKSLF VRFENLVDKN LFNQASTGIG
     LSLVKELVEM HKATISVDSR LGEGSCFKVD FLKGKEHYDK ETEFILEDAD APVRMGQVVD
     IANSSIQSET LIPDDSEKIE AVYEEDAAKE ENSKELMLLV EDNQELREFL RSIFSPMYRV
     VEAADGREGA NKALKYLPDI IISDVMMPEK DGIEMTRELR ADMTTSHIPI ILLTAKTTIE
     SKLEGLEYGA DDYITKPFSA TYLQARVENL LMQRKKLQSF YRDSLMHINM SVTSGELVAL
     TKAMAEEERK IVPEREEEQT QLQSQQQPTI PDMSPNDRKF MDKLVELMEQ NMDNGDLVVD
     DLVRELAVSR SVFFKKLKTL TGLAPIEFIK EIRIKRATQL IETGEFNMTQ ISYMVGINDP
     RYFSKCFKAQ VGMTPTEYKE KIGR
//
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