ID Q8A0B0_BACTN Unreviewed; 1511 AA.
AC Q8A0B0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BT_4111 {ECO:0000313|EMBL:AAO79216.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO79216.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO79216.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000313|EMBL:AAO79216.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; AE015928; AAO79216.1; -; Genomic_DNA.
DR RefSeq; NP_813022.1; NC_004663.1.
DR RefSeq; WP_011109105.1; NC_004663.1.
DR SMR; Q8A0B0; -.
DR STRING; 226186.BT_4111; -.
DR PaxDb; 226186-BT_4111; -.
DR EnsemblBacteria; AAO79216; AAO79216; BT_4111.
DR GeneID; 60925286; -.
DR KEGG; bth:BT_4111; -.
DR PATRIC; fig|226186.12.peg.4177; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2207; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR InParanoid; Q8A0B0; -.
DR OrthoDB; 1108380at2; -.
DR Proteomes; UP000001414; 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; IBA:GO_Central.
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; IPR000959; POLO_box_dom.
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; 3.
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; 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; PS50078; POLO_BOX; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:AAO79216.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001414};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AAO79216.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1511
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004304986"
FT TRANSMEM 911..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 545..615
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 957..1174
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1234..1349
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1409..1508
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1378..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1282
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1511 AA; 172249 MW; EFB0B363C1851BD0 CRC64;
MIKRILYLIL LCLTAPVVQA QQHSFFTHYS TEDGLSQNTV MSMLQDHKDN LWFATWDGIN
RFDGYNFKTY KARQGNYISL TNNRADRMYE DRYGFLWLLT YDNRVHRFDP KTETFEQVPA
AGEEGSTYNI HAIQVLPDGT VWLLTEHDGA IRVVTLPQKN YTTKSDIYST KSGLFPADHF
YQVYQDKAGN HWLLTDNGLG MIRPGEQQPV NYFVETKGKQ DGMNQAFYAV RECEDDICFA
SDRGRIWCYQ KQGGEFRLLE LPTKARITSI HTVSNGNTVV TTDSDGFFLC NLKTNKHTHY
SPVTCKELSA QPILSAYVDR TSEVWFEQEE PGVVVHFNPA TGVVRREQMR VEYSNADRSR
PAFHIHEDVH GHIWVHPYGG GFSYFDRDRN CLVPFYDDLG SNNWRFSNKI HAAFSDKQGN
LWLCTHSKGL EKVTFRNVPF SMLTPVPHEY ESLSNEVRSV CEDKQGNLWV GLKDGMIRLY
DSNRKFIGHL TGNGTISMTG TPMEGTAYFI MQDSKGIIWI ATKGNGLVRA EQISPTSMSY
KLTRYQHDSN DMYSLSDNNV YCVYEDHHGR IWAATFAGGI NYISQGEHGE TVFINHRNNL
KGYPIDVCYK ARFITSDNNG RLWVGTTTGA VAFDENFKKP EDIQFHHFSR VPNDTKSLSN
NDVHWIIATQ QKELYLATFG GGLNKLISIS ENGHGEFKSY SVLDGLSSDV LLSIREDHKQ
NLWISTENGI CKFVPSGERF ENYDERSISF RVRFSEAAST LTSGGDMLFG TSNGLFMFTP
DSIRKSSYVP PVVFSKLMVA NEDVIPGEKS ILKVDLDDTQ ELVLSHDENI FSVQYAALDY
TNPQNIQYAY ILDGFEKQWT FADRQRSVTY TNLPKGDYIF RVRSTNSDGV WVDNERILNI
TILPSFWETP LAYVLYVCFV LLIIFVAVYI LFTIYRLKHE VSVEQQISDI KLRFFTNISH
ELRTPLTLIA GPVEQVLKND KLPADAREQL VVVERNTNRM LRLVNQILDF RKIQNKKMKM
QVQQLNVVAF VRKIMDNFES VAEEHNIDFL FQTEKEALNL WVDADKFEKI VFNLLSNAFK
YTPNGKMITV FIREDEGTVS VGVQDQGIGI AENKRKSLFV RFENLVDKNI FNQASSGIGL
SLVKELVEMH KATISVDSRL GEGSCFKVDF LKGKEHYNSS VEFILEDSVA PLSMERIVDI
ANSSLQTEAA IADAPDLEVS AVKEEAEESS SKELMLLVED NQELRSFLRS IFASTYRVVE
ASEGMEGWSK ALKYLPDIII SDVMMPEKDG IEMTRELRAD MTTSHIPIIL LTAKTTIESK
LEGLEYGADD YITKPFSATY LQARVENLLM QRKKLQNFYR DSLTHVTVSE TPVAQGETLA
GHASAEPVSS AAEEPAMPEM SPNDRKFMDK LVDLMEQNMD NGELVVDDLV RELAVSRSVF
FKKLKTLTGL APIEFIKEMR IKRAAQLIET GEFNMTQISY MVGINDPRYF SKCFKAQVGM
TPTEYREKVG R
//
