ID A0A1M6J6U7_9BACE Unreviewed; 1364 AA.
AC A0A1M6J6U7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444350_12719 {ECO:0000313|EMBL:SHJ42391.1};
OS Bacteroides stercorirosoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871324 {ECO:0000313|EMBL:SHJ42391.1, ECO:0000313|Proteomes:UP000184192};
RN [1] {ECO:0000313|EMBL:SHJ42391.1, ECO:0000313|Proteomes:UP000184192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26884 {ECO:0000313|EMBL:SHJ42391.1,
RC ECO:0000313|Proteomes:UP000184192};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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};
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DR EMBL; FQZN01000027; SHJ42391.1; -; Genomic_DNA.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR Proteomes; UP000184192; 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; 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; 2.
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; 3.
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 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 798..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 852..1069
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1115..1230
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1262..1361
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1163
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1364 AA; 156224 MW; 899C25DC58767A52 CRC64;
MICLFCIIFR GQIYKLNFMF PKMMQNIAKR LFLLFILLSG FIAASAQNVT LNSYSVKDGL
SNSTVKAICQ DAKGYIWIGT KNGLNRLDGY EIKNYYHLPS REVKQPNDIV SITQLSDGLF
WIGTFSGIVL FDPMQEKFID LQERYAGKEF PSSVVVGLHE DPKKNIWVAT KQGLYVFKND
GTCSYVKDLR ETYIHMMAVA DPYALLLDIV NQGLALYDVR TERYKILHKN EKRFSLMKGF
TDSKGRIWLG EELKNFYRYF PKEEEIRPVS YTVHPDVPIE SNYIHDITEY NDSTLLLATD
RGLVAYDIAR SVFYTEINQH LSINNRMMTV YKDKQGALWM GTFSQGAIYY HPQLFTFTHH
PLTASTKPAT GIQVVGSLAE SQGKLWIGHS KGLISMNLTH SNQIEEVNIS GNNSPKHDTD
LYYVYQNSKD ELYLYFLNMG VYSLNLKTRS IAKVITPMTG EEQIRAMARD AENHLWIAED
DLSYWDEKTQ KLDRNLSTNY NAATRYMLTQ DILRHGDDMI VGVRTNGLWV FKYQPENPEH
YFKGERTAFE ELNDKNISVL YEDNAGNIWI GTYDNGLYKC NLEKQKIHHY NKDNGLVHNS
ICAILEERTS KDIWVSAING LSQIKPDGTI VNFTRGNGFP LNEVSHKSLV QASNGHIYIG
GNNGLAELDP ARLSHKQVTA PLVQISLVES LNSKNAPGHI EINNFNNDNK IDLPYDNSSI
RIKYSALDFI SPKGYKYAYQ LKGMDKEWHY IENNEVIYSN LPAGKYVFSI KACNNEGIWS
TVETTIIISV HPAFWATWWA KTIYILFIII FLMVLARYFY EKKTAKYKQK IEQIEKENIE
KNYQMRIELF TNFSHELRTP LTLITGPVDD IINDEQLPSS LKYPMKQIQK NANRLLLLVN
QLMDFRKLEH GAMQLKLSNL NVAIFISEQI DSFSELLNKH ELTISYSNNY YGNDLWVDVD
LMSKVMFNLL SNAIKHSPKG GKIQLTSNVE EYCVIFSVKD CGEGISPENQ SKVFDPFFQI
GNGNKNEMFG SGIGLNLVRY VVKLHSGKIW LESTPGQGTT FFIRLPLGKD HYNSSNVIYT
DQAITHTLKV EKNSVLSVDP EYHQEMPEES DNRLRILVVE DDEDMRQYIV SKLSKLYSVQ
EAPDGKKAIE IAKEQMPDLI VSDIMMPVMD GLELCRTVKN DMTLAHIPVV LLTAKSLEEH
IKDGYQALAD DYILKPFNAQ ILLAKIESLI KNREKLRNIF CQKLGTTEVP VREITVEDPF
MKKLVELITE NAQDPDLSME VLYNKLGMSR TQFFRKIKAI SDLSPNKLIL NIRMKMAVEK
LQAGGMTIAE VAYEVGFSDP AYFSKVFKSV FNQTPTEYIK NIGK
//
