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Database: UniProt
Entry: A0A374V9G8_9BACE
LinkDB: A0A374V9G8_9BACE
Original site: A0A374V9G8_9BACE 
ID   A0A374V9G8_9BACE        Unreviewed;      1365 AA.
AC   A0A374V9G8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DXC10_09155 {ECO:0000313|EMBL:RGM47414.1};
OS   Bacteroides sp. OM08-11.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=2292284 {ECO:0000313|EMBL:RGM47414.1, ECO:0000313|Proteomes:UP000262405};
RN   [1] {ECO:0000313|EMBL:RGM47414.1, ECO:0000313|Proteomes:UP000262405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM08-11 {ECO:0000313|EMBL:RGM47414.1,
RC   ECO:0000313|Proteomes:UP000262405};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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};
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:RGM47414.1}.
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DR   EMBL; QSTJ01000004; RGM47414.1; -; Genomic_DNA.
DR   OrthoDB; 9809670at2; -.
DR   Proteomes; UP000262405; 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; cd00075; HATPase; 1.
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; 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; 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; 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   SUPFAM; SSF101898; NHL repeat; 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:RGM47414.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000262405};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:RGM47414.1};
KW   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..1365
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017036449"
FT   TRANSMEM        789..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        913..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          843..1078
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1111..1226
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1258..1357
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1159
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1365 AA;  156263 MW;  6C7431AAFA49E529 CRC64;
     MKKFVLLLFS LLTILQIFAQ NDNETFYFSN LNLKDGLSQI SVIKILQDSK GFMWFATRNG
     LNRYDGSEFI VYKHVPGDSL TLSDNNIISL VEDKNRNLWV GTARGLNKLD LKTNHIKRYS
     DKKHGALAKV DIRSLFVDSR NRLWVGTSRG LYLYVREMDM FQRLDLNGKI KDEYISVIHE
     TKEHQILIGT ATKGLFVCDM NMKEQKHFTM DTPNLRLPDN YVGTLYEDLE GHIWGGSNAG
     GLFRIDIEKE NIITYHKGNS ILTTNSIRCI AESHDRLLIG TFDGLYSMNL SDNSFWKHTD
     ASLERGNLSH FSIYSLFVDS SQTIWVGTYA GGVSYSSRFN NRFDFHDPTS VFDALFGIYG
     SMVCTEGGCL YMATEGRGLL DYNLNNSKYY YYPIDNSSRL QYSQNIIKGL LLDGNTLWCG
     TNKGTIYQFD TRTKQYKLYY QLPKEMSIYA MTPAHDGGLW IVGSDPKTGL IHLSAKKIFL
     DKFPLHDGKD SCQIASSRCI LKLRDGVLLI GTRNNGLVKY DANKQEITYY NTDAKKPFSL
     LNNYVTSIIR DASDRIWIGT FGGGISLYDE YKGVLKTITR EQGLIDNDVC AIVEDRDHKL
     WISTSNGISE FDQEKEQFIN YNSLNGIGVY EFTPHSGMLL PNGEVCFSGN NGFVTFNPQE
     LQLNSFVPPL VFTRLVVNNE VIEVGDETGI LSSVLDDVKE IDLDYSQNNI SIGYCALNFV
     FARQNQYAIF LEGYDKDWNY IGNRREAYYT NLSPGTYEFK VKASNNDGVW SQETRKIRIV
     VHPPIWETWY AYLFYVVTFV SVLVLIMYYI FKKQKLEREL QFQQKEQQQL EEFHQAKIRM
     FTNFSHELRT PLTLIIAPLQ ELVAMPEFSS VVKNKLGLIF SNAQRLLLLV NQLMDLRKNQ
     EGKLKLRIIK SDMYLFLLEI YYAFNHLAAK KSINFTFERK VEQLMAWFDK TLIEKVVFNL
     LSNAMKFTPN GGKVVFSLSQ ISSSALPAEY QSELSKLPVN TEFVCLSVAD SGKGIPDEEI
     KNIFAPFYQG EDDNKENVGT GIGLSLTRSI VHLHHGIITV SKNQPTGTVF NVYIPISSFV
     YEEDQLVKEE TVEDVIPVDK AMHFDIEKKW TILLAEDNDE VRRYVKECLE PYFYILDVDN
     GKDALELSLE KYPDLILSDI MMPKMDGLEL CSRVKQDLQL GHIPVILMTA KSMVVHIKEG
     FSVGADDYIV KPFCMDVLIC RINNILESRE KLKKLYGKKF SPEAMGIEIV SGDDRFTQSF
     FELIEKNISN PELGIDLLSQ ELGLSRANLY RKLKAVTELS PTELIRNKRL EVAAKLLLES
     DYTVSEVAVY TGFNSHAYFT NCFKSFYGYS PSEWVQRHHE NNENV
//
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