ID A0A3P2ADW7_9BACE Unreviewed; 1368 AA.
AC A0A3P2ADW7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EII33_04270 {ECO:0000313|EMBL:RRD92360.1};
OS Bacteroides heparinolyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=28113 {ECO:0000313|EMBL:RRD92360.1, ECO:0000313|Proteomes:UP000279562};
RN [1] {ECO:0000313|EMBL:RRD92360.1, ECO:0000313|Proteomes:UP000279562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1047_COT-310 {ECO:0000313|EMBL:RRD92360.1,
RC ECO:0000313|Proteomes:UP000279562};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-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:RRD92360.1}.
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DR EMBL; RQYF01000011; RRD92360.1; -; Genomic_DNA.
DR Proteomes; UP000279562; 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; cd00063; FN3; 1.
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; IPR003961; FN3_dom.
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; 6.
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; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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:RRD92360.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000279562};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:RRD92360.1};
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..1368
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018109883"
FT TRANSMEM 794..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 848..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1121..1236
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1266..1365
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1169
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1368 AA; 155391 MW; 8E2D074D7477F199 CRC64;
MKRLYLFLWG ICMVCLSAAA QNYMFKCLEV KDGLPNNQIN SICKDSRGFL WFGTASGLAR
YDGYRFRTFR HDDSRTTSIP DNFVENIVED SEGRLWMRIG ETNYTFFDPV AETFENDMRG
YMWNIGINGV PQEVMVDKEK TLWFYVPGVG CYRYRAGEKK AEGLLFTTGG LPQGNITGMI
DSKEGILLAY SNGRIVCIDS RRMALKWTLT DITEMVGEEY VETFSLFVDR DEDLWIYGAP
GLWVYNLKSK EWKKNRSDRI SNLSHNMIRS ITQDRKGQIW LGKDQEGIDV LDKKTGKITS
LISHPDNERG LPHNTIMELY EDAAGIMWVG TYKKGVAYYD ESIYKFALSP LGDVNAIEDG
RDGTLWLGTN DGGLVHWNPQ SGEKNTFLRR GENSLTANVV VSLLKAKDGR LWIGTFWGGL
DCYDGHRFVH YRHQPGNPNS LSNNNVWSLA EDEEGNIWIG TLSGGVQRLN PKTGVFTNYN
VATCGLISDY IASICMGRNN RLIIGTASSG ISILDLNTGR ATNYVGTKSG NARFSNQSVN
QVYEDSRGLI WIATRDGLNL YDPVNDGLQV ISLPQEISGR FISGIVEDKH RNMWVTTADG
VVNMVVLQDK RSQEYTFHFH VYNDKDGLQG SEFNLRSIER LASGEVVMGG LYGINIFNPD
VIKYNRTQPK VIFTDFRLFN EEVEVGREYG GRVVLDKSLN HIGELTLDYR QNVFTVVFAS
DNYVLPEKTH YIYKLEGFDN DWMTSASDMR RATYTNLAPG TYVLRVKAVN SDGFAGTEEA
VLKIVILPPF WQTAWAYIFY VLLLVGIIYL SIRAVERKER NKFKIRQMEQ DARKMEEVNQ
MKFRFFTNVS HELRTPLTLI ISPLESMMKE VSDDKQLGRL TLMHRNALRL LNLVNQLLDF
RKSEVAGLHL TSAEGDIVAF VRHICASFLM LSEKKNVHLT FYSAVESLNM LFDEDKMGKV
VMNLLSNAFK FTPEGGRVDV SVEVLKGEPD KLLLKVSDTG TGIKDEDKEH IFERFYQVDH
PNPNLQSTGS GIGLSLVHDF VTLHEGTVQV LDNVSVGSVF LVTIPIKQVS REGAVSKSGR
KKEAEKVFVE SEIEQILEEE NEALSDDMDD TTDGGDKEQP LVLVVDDSDD LVAFMKDSLS
LYFCIQTASN GREAWRLIPD LQPDIIVSDV MMPEMDGNEL CRWVKTDKRT ENIPVILLTA
KQAVEDKVES LTIGADDYVT KPFNVEVLIL RMRKLIDLYG KRRQRLRIEP EPSRIVITSL
DEQLVADAIK YVEANIGRSD LSVEELSREL GMSRVHLYKK LSQITGKTPI EFIRIIRLKR
AAQLLRESQR NVSEIAYQLG FNNPKYFSKY FRDEFGVLPS VYQEREGK
//
