ID E5CCC0_9BACE Unreviewed; 960 AA.
AC E5CCC0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 2.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BSGG_3093 {ECO:0000313|EMBL:EFS32393.2};
OS Bacteroides sp. D2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=556259 {ECO:0000313|EMBL:EFS32393.2, ECO:0000313|Proteomes:UP000003135};
RN [1] {ECO:0000313|EMBL:EFS32393.2, ECO:0000313|Proteomes:UP000003135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EFS32393.2,
RC ECO:0000313|Proteomes:UP000003135};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA Sibley C., White A., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. D2.";
RL Submitted (OCT-2011) 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:EFS32393.2}.
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DR EMBL; ACGA02000052; EFS32393.2; -; Genomic_DNA.
DR RefSeq; WP_008999773.1; NZ_JH636024.1.
DR AlphaFoldDB; E5CCC0; -.
DR HOGENOM; CLU_000445_28_7_10; -.
DR OrthoDB; 358279at2; -.
DR Proteomes; UP000003135; 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; cd06308; PBP1_sensor_kinase-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.250.850; -; 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 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; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF13407; Peripla_BP_4; 1.
DR Pfam; PF00072; Response_reg; 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; SSF58100; Bacterial hemolysins; 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; SSF53822; Periplasmic binding protein-like I; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 428..646
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 714..829
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 859..958
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT COILED 363..421
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 762
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 960 AA; 107629 MW; 6659AEAC49E9F6C1 CRC64;
MIEAMKYTKW ITVLFCLLGL AACRQDAPRF RIGVAQCSDD SWRHKMNDEI LREAMFYDGV
SVEIRSAADD NRKQAEDVHY FIDKGVDLLI ISANEAAPMT PIVEEAYQKG IPVILVDRKI
LSDKYTAYIG ADNYEIGRAV GNYIASSLKG KGNVVELTGL GGSTPAMERH QGFMAAISNY
PDIKLIDKAD AAWEREPAEV EMDSMLRRHP KIDAVYAHND RIAPGAYQAA KKAGREKEMI
FVGIDALPGK GNGLELVLDN VLDATFIYPT NGDKVMQLAM NILEKKSYPR ETVMNTAVVD
RTNAHVMQLQ TTHISELDQK IETLNGRIGG YLSRVATQQV VMYGGLVILL LVAGLLLVVY
KSLRSKNRLN KELSEQKKQV EQQRDKLEEQ RDILEEQRDK LEEQRDQLIQ LSHQLEEATH
AKLVFFTNIS HDFRTPLTLV ADPVEHLLAD SSLSEDQRRM LLLVQRNVNI LLRLVNQILD
FRKYENGKME YTPISLDILS SFEGWNESFM AAARKKHIHF SFDYMPDTDY RTLADVEKLE
RIYFNLLSNA FKFTPENGKV TVRLSSLTKD DHCWIRFTVA NTGSMISAEH IRNIFDRFYK
IDMHHAGSGI GLALVKAFVE LHKGTITVES DEKQGTIFTV DLPVQTCETV VSENSPAFSV
PATSVTSTDA ATSAVAGAPV TPATSGYSGS SSLNDALTYE EEELEKSYDS SKPCVLIIDD
NADIRLYVHG LLHTDYTVIE AADGSEGIRK AMKYVPDLII SDVMMPGIDG IECCRRLKSE
LQTCHIPVIL LTACSLDEQR IQGYDGGADS YISKPFSSQL LVARVRNLID SHRRLKQFFG
DGQTLAKEDV CDMDKDFVEK FKALIEAKMG DSNLNVEDLG KDMGLSRVQL YRKIKSLTNY
SPNELLRIAR LKKAASLLAS SDMTVAEIGY EVGFSSPSYF TKCYREQFGE SPTDLLKRKG
//
