ID E5WVP8_9BACE Unreviewed; 1239 AA.
AC E5WVP8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1016_00750 {ECO:0000313|EMBL:EFV30858.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV30858.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV30858.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV30858.1,
RC ECO:0000313|Proteomes:UP000003246};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL Submitted (OCT-2010) 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:EFV30858.1}.
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DR EMBL; ACWG01000008; EFV30858.1; -; Genomic_DNA.
DR RefSeq; WP_004293184.1; NZ_GL622539.1.
DR AlphaFoldDB; E5WVP8; -.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000003246; 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 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; 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; IPR011044; Quino_amine_DH_bsu.
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; 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 SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 709..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 748..965
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 995..1110
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1142..1239
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1043
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1239 AA; 138590 MW; 59D676E7F29141FE CRC64;
MREITAAVRD DDGFIWAASR SGVLRVASDD YRLYQLPFAT TDVLQLKMAS RGSLLVVATQ
NGQVFRYNRI LNKFEQWFTL SSLLGNDNWV TNLLIDVDGK VWISTSIGIF FWTGKEVARA
FDDMAGVSNI ALLEDCHALA FVQSSIYHID TRKHTYTKLC GHLPTLISSA RFDAHAGRVW
VGTYDAGLWE YELTTQTARK VAVPHFPQLI VRDILIPDST SLWVAVDGGG IWILDSKACR
VQQVIREDVD KPSSLRGNSV YSLLADNHNR IWVATNGGGL QYTETASVDV EHLIHGINNS
QSLHNNEVNH IMADSRGNLW IATNDGISLR NANTLQWHQL YSGRQRAFLS LAADKKGHIY
AGTYGEGVYV LDEVTGRELR HYTSDDGNIF GAGGFVFAAY TDSQGDVWLG GVRGSVYCCN
SASGKLRAYD TQPVYCFAEL SPGQILLGCA YGLLLMDKET GKFDVLLSGN TIHDIAVDGH
TIWVCTSGNG MIGLDMRTAR QTHITTQQGL PSNYIKSVLL ADNNLWIGTD NGICCYNLTN
KQIRTFGTQQ NLANVSFSVN AACQLPDGRL AFGSNSGAVL FYPDRIDTVS ALGRIYFSDI
RVSGRSIREI ADFNLSVPID SLSVLHLSYP QTSFTLSVLP LGCVGKSVAF SWKLMGQDHV
WSTYTTSRYI NYTNLPAGKY TLCIRLSDGS LLSERQMSIV VDPPFWKTIW FRLLLTVVII
GVLFLAVRYY MQYLRRRYSD EKIRFFTRMA HDIRTSLMLI KAPIEELHKE KELSSWGAKC
LTLASEQTAR LSDTATQLLD FEKLDIGCEQ PQFTDISLTD LIRRRAGIYA SYAAGQQIDI
LADLTPEDYW IQADARMLER VVDNLLSNAV KYSSSGGRVE VSFIGKTDEW ILRVKDYGMG
ISKAAQRKLF REFYRSDNVV NTQIVGSGIG LLMTKKYVSI HNGKIAVTSE LGVGTTFDVT
VPLRPASKTK AADIPAISNK VDEPVMDDVE AHDMHILIVE DNHALREFMV HPLREHFRVT
TADDGQQAWE MMNELQPDLV VSDVVMPRMD GFELCRRIKS TYETSHIPVI LLTALSDKTN
QLHGLELGAD NYLTKPFDMA LLASRITSII RNRRTVLQKA IEVKRDDAHS IVANRMNDEF
IKKAVECVRA NIANENFGKE DFASALALSQ SLLYKKIKAL TNLSVVEFIR SIRLNYAMEK
LRSGEYNVTE VSEMCGFSTP AYFSKVFKEY FGKTPTEVM
//
