ID W4UQI8_9BACE Unreviewed; 849 AA.
AC W4UQI8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JCM10512_1499 {ECO:0000313|EMBL:GAE83241.1};
OS Bacteroides reticulotermitis JCM 10512.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE83241.1, ECO:0000313|Proteomes:UP000019131};
RN [1] {ECO:0000313|EMBL:GAE83241.1, ECO:0000313|Proteomes:UP000019131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE83241.1,
RC ECO:0000313|Proteomes:UP000019131};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT Isolated from the Gut of a Termite.";
RL Genome Announc. 2:e00072-14(2014).
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:GAE83241.1}.
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DR EMBL; BAIV01000007; GAE83241.1; -; Genomic_DNA.
DR AlphaFoldDB; W4UQI8; -.
DR STRING; 1445607.JCM10512_1499; -.
DR Proteomes; UP000019131; 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; 1.
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; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019131};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..550
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 599..714
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 747..847
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 647
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 849 AA; 97313 MW; 592B4E88B3CE8FAC CRC64;
MWMALTMGGV ICIHLPSGEV TRYTSESSLN AAVGKFKIVH IFEDSAQEVY FSTIGSGVFK
YNEKDRSFKS YSTSNQLLPS DYCYYICESI DSHRLFFLHG KGITVYNKDK REVENTYHLF
NQTYSQGSAL FRVEKGSVLL LGTNGLAIFQ ERSLKALPAK NFLNFDKLLI FNKEVVPNDG
SGILTDILAR TSDIYLNFKQ NNVTIEFATF SYNNDRNCLF EYRMDGLDKV WTQTNGTLIT
YTSLPPGDYT LRVRVLESKQ IEAKEISLKL HISAPFYATI WAYLIYFICL SGLLLTFIRF
KMRQAALKSS LEFERKEKER IEELNQVKLR FFTNISHEFR TPLTLILGQI EALMQMDKLG
SMVHNRILRI YKNAWHMRNL ISELLDFRKQ EQGYLKLKVE EQNLVPFTRQ IYLCFYEYAQ
NKEITYRFMH LEDTVSAWFD SKQLQKVIFN LLSNAFKYTS NKGSITVEVR KVASQAVVIV
SDTGSGISQE HLSKIFDRFY QTDTTSFTTL GTGIGLALAK GIMTMHHGTV DVESEIGKGA
KFTLSLPLGN RHFSDEEMAS TEGRESAILP EIASLPFYST PIEEAVTNAE FSEEENKPVI
LLVEDHEELL LMLKEIFSPM YEVYIAYNGR EGWEMVQQIQ PDLIVSDVMM PEMSGKELCY
RIKTNVELSH ISVVLLTAQT SVEYAVEGFM FGADDYVTKP FNVKVLVARC NNLLNNKKRL
MSYYAGKVIM ETPALEAVNE RDKEFLAKCV SIVKTNFENL QFDVTMLASE LCMGRSKLYM
EFKGITGLTP NEFILKVKLD EAMYLLNNHF DLNISEISMR LGFSSPRYFS KSFKAFFGVT
PQSVRSKKK
//
