ID F5IWG6_9BACT Unreviewed; 1329 AA.
AC F5IWG6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9455_01433 {ECO:0000313|EMBL:EGK02476.1};
OS Dysgonomonas gadei ATCC BAA-286.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGK02476.1, ECO:0000313|Proteomes:UP000004913};
RN [1] {ECO:0000313|EMBL:EGK02476.1, ECO:0000313|Proteomes:UP000004913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGK02476.1,
RC ECO:0000313|Proteomes:UP000004913};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286.";
RL Submitted (APR-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:EGK02476.1}.
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DR EMBL; ADLV01000017; EGK02476.1; -; Genomic_DNA.
DR STRING; 742766.HMPREF9455_01433; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000004913; 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; 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; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR011110; Reg_prop.
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; 6.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000004913};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1329
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003324080"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 838..1055
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1077..1191
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1223..1322
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1124
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1329 AA; 153033 MW; 4196B2A228AD5CEA CRC64;
MRLNTLKFFL CLSLCFVITG LSSQSTQYYF SHYGIREGLS QNTVNAILQD RTGFLWVGTK
DGLNRFDGFS FRTFKRDILD KNSIGNNYIK VLHEDNRGKI WVGTDAGIYV YDPYTEQFSQ
FLVQADNKVV INKTISAIEG NGSYIWIAVE SQGIFCYDVQ SGLLRNFDLK SHDISSNIEC
LKEDRNGVLW LGSYGEGLFY SKDNLKTIRE FTDDNGEKVF RDDVILKIIP GAYNCLYVGS
VKEGLKELSL SSGKVRDLLQ IDNNNEKIFI RDIMINSDNE LWLGTESGIY IYNLRTNNYL
HLESSFYDSY SLSDNAIYCL CKDREEGIWI GSYFGGLNYY PKQYTHFNKY YPTDTSNGLR
GKRVREFCAD PSGLIWISTE DGGLSNYNPQ TNKISFFEPS RAFSNVQCLL PDGDNLWVGT
FSKGVKVINR NTGHIKSYNK GNTSNSLNDD NIFAMLRTSD GTIYLGTLFG LLKYNRATDD
FFVIPELKGK FIYDIKEDRH GDLWLATYSD GVFCYDINKK KWKNYLHNET DEKSLPYNKV
TSIFEDSRHQ IWITTQGRGF CRFDPSTETF IRYDERNGLP NDVIYQIVED DKGLFWITSN
KGLICFNPVD NFIKNYTVVD GILSNQFNYR SGFKSEDGSL FMGSIDGFIR FEPKDFSESK
YKPTPVITDF LLYNKRVSVG ERKSPLQRSI IYTDSLILNS KQNSFSFRVA ALSYLSPHTN
ILKYKLEGFD KDWLLMTESP LINYSNLKYG DYVFRLKISD PTMPSIENEK ILFIRILPPF
YLSPWAYVLY VLIFGSFVYY IVYNIRKRAT MRERREMEKF EQQKALEIYD AKIRFFTDVA
HEIRTPLTLI KGPLENILLT DYIDDMIRDD LNIMNHNTDR LLNLTNQLLD FQKIESKGLQ
LSFTECNISD ILRGCYLQFK LSTQQMNLNF VLRLPDKDLF AHIDKEAFTK IISNLFSNAM
KYAQTYIEVK LDVDDEKREL RVVIKNDGNI ISPDMREEVF KPFVRLNNIE TSKPLPGTGI
GLALSRSLAK LHQGSLYIED YADCNSFCLV LPMTVYDEKA LPLPVIVQPE DSSSRLAILI
VEDDPELLAF IVKQLSAYTI FTATDGNEAL NVLDSNIVNL IITDVMMPHM DGFELCRILK
SNIDYSHIPV ILLTAKTNLR SKIEGLEAGA DMYIEKPFSV EYLRACASNL IHNRIKLKEI
FVNSPLVAAN SMAFTKADED FLKKMNEIIL DNIDNPEFNM DDMVGTLHMS RSVFYRKIKG
ILNMNPNEYL RLERLKKAAE LLLAGNSRIN EVCYLVGFNS PSYFAKCFQK QFGILPKDFV
NSKKQMPRD
//
