ID A0A1M5ELD4_9BACE Unreviewed; 1363 AA.
AC A0A1M5ELD4;
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=SAMN05444349_1363 {ECO:0000313|EMBL:SHF80049.1};
OS Bacteroides faecichinchillae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871325 {ECO:0000313|EMBL:SHF80049.1, ECO:0000313|Proteomes:UP000184436};
RN [1] {ECO:0000313|EMBL:SHF80049.1, ECO:0000313|Proteomes:UP000184436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26883 {ECO:0000313|EMBL:SHF80049.1,
RC ECO:0000313|Proteomes:UP000184436};
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; FQVD01000036; SHF80049.1; -; Genomic_DNA.
DR RefSeq; WP_025075967.1; NZ_SSTN01000004.1.
DR STRING; 871325.SAMN05444349_1363; -.
DR OrthoDB; 1116352at2; -.
DR Proteomes; UP000184436; 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; 4.
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 Kinase {ECO:0000313|EMBL:SHF80049.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184436};
KW Transferase {ECO:0000313|EMBL:SHF80049.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 800..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 854..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1113..1228
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1260..1360
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1161
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1363 AA; 157050 MW; E9772C89887025E3 CRC64;
MPKFCLCLIL WILGIFYSGS VLRAEAVSDL KFIPIQSKLL PSNEVRKLYQ DSDGYIWIPT
YNGLVRYDGY NIITYGLYNG IDESFNSYLN AVVEDDSKNL WIATEKGLYQ LNKITGKLSY
IRSDELGQLN AADLLYGTGK SLWIGGDKGL FRKGKDEDFE RIDLKEPSGK RVLHISSIME
DSRQNLWITA WEQGLFRYDI KNKKLYSYID PVLRNANVVF EDANHSIWVG TWGKGLLKLN
NPYTSGSMYY KQYIHDEKNS NSLLDDIIYD IEQDNEHRLW IGSRSGLSIL CNEQDINSFK
NFVPDGEYGS LPYNEVSSIL RTRDNLMWIS MFGGGFCKIQ TESNKYGVDN LEIVKEKYNT
NSVRSICQAG ENEFWMGIIG FGMIKYNLET QNCVNYVDIP EFKSLSYTST VDAIIKRKNG
EICFGTWNAG LWFYNETDRK ITLLNQYVNR KFKDDCIHVL REDSEGNLWI GTRKGVYILD
TQGQFYTLSE WLHFDTDLVS SNIFDIKEDQ DKNIWIATNY EGVSRINLST RQYKKYPVIG
KKEIYNTNCL LVDSHQRIWV GTMWSGLAYY QKETDSFVTV SSISTIENKG ILNILEDDNG
RIWITTNSAV LSFEVNDSFQ MEKINYYTVS NGASEFFFNK NASFKMPDGR IIFGGSQGLR
IFESSQIVED TPLFYSLAFT DFRIHNQSLR DFPEKKREKL AKYDIDYTKE ITLTHDKNNF
YIEFSLLNYE NPQENLYSYQ LEGYDEKEVV VDAQQRFAIY NNLPAGTYTF RLKGTSASGV
WSKHEKTLTI HILPEPWKSW WAYLLYFLIG GTLFYFVIRF IHYRWKMQHE IQISKLEKQK
IEEINHVKLQ FFTNITHELM TPLSIILASL ENLKNNTGDQ SSLYSIMSSN VIRLMRLIQQ
VLEFRKVESG NLKICVSSGN ISEAVENCIE AFAPLVAKKL LKIDFLSDPE IIIGYYDSDK
LDKIIYNLLS NAAKYTPEKG KISVNLRLIE DSGIQIECIN TGEPMSKGKM NTLFQRFYEG
DYRKYHTIGT GIGLSLVKDL VEKHHGEITV QSEENIGNCF RIVLPITKES YQEDEIDDSV
KSQIVSGLPY IMCESGANTE ELERIDGVQS DYTILIVDDN EELCMLFSNL FANYFHVKTA
YNGKQGLEIL ESTSIHLIVS DIMMPEMDGI EFCQTVKSKF EFCHIPVILL TARGTEESQI
EGYNSGADGY ISKPCNFSLL YAQIMNLLKK QERKGADFRK QIVFEVGKLE YTSMDESFIQ
RAIDCVNSHL GDCEFGQQEF VREMGTSRTV LTEKLKSLTG LTPSIFILNV RLTAACKLLE
EQKKMRIADL AYSVGFNDPK YFSTCFKKKY SLSPKEYMDR LQS
//