ID D6D5V6_9BACE Unreviewed; 1415 AA.
AC D6D5V6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BXY_03300 {ECO:0000313|EMBL:CBK65604.1};
OS Bacteroides xylanisolvens XB1A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK65604.1, ECO:0000313|Proteomes:UP000008795};
RN [1] {ECO:0000313|EMBL:CBK65604.1, ECO:0000313|Proteomes:UP000008795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB1A {ECO:0000313|EMBL:CBK65604.1,
RC ECO:0000313|Proteomes:UP000008795};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Bacteriodes xylanisolvens XB1A.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK65604.1, ECO:0000313|Proteomes:UP000008795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB1A {ECO:0000313|EMBL:CBK65604.1,
RC ECO:0000313|Proteomes:UP000008795};
RA Pajon A.;
RL Submitted (MAR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929033; CBK65604.1; -; Genomic_DNA.
DR KEGG; bxy:BXY_03300; -.
DR PATRIC; fig|657309.4.peg.3002; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_007691_0_0_10; -.
DR Proteomes; UP000008795; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR033405; DUF5112.
DR InterPro; IPR033406; DUF5113.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF17139; DUF5112; 1.
DR Pfam; PF17140; DUF5113; 2.
DR Pfam; PF02518; HATPase_c; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CBK65604.1}; Membrane {ECO:0000256|SAM:Phobius};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:CBK65604.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 282..315
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 561..795
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1194..1415
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1415 AA; 163924 MW; B814A9BFC4DAC717 CRC64;
MVPTKEVRLI DSLNGKAYTY RYRSLDSSYK YANEAYQQVN FYKSGKAEAS NNLGFCAFMA
MDFDRAEALH KEVYKLTKNE LELLIADIGL MKICQRTAMN KEFYDYRNSA LRRMKRIREE
SDLFADRHEA LRLDYAFTEF FIVSSIYYYY LQQRQEAIAS LNQIPEDEVL ADTNQLLYYH
YIKGSASLVE ATKPEDRKMR EFDQLYITWR TAVQTNHPYF EGNGLQGLAN LMVSSNNFEL
FRTRRGYALD QFGFPVDSLL PLRMAQLALE KFREYNDLYQ IAGAYVSIGK YMNEHGRYSE
ALDTLTKALD CVNQHHMLYY HHAVDTLDKL RIYAEGDTTY TGVPWIMEED VRTVPEWISR
IREQLSVSYA GLGMKYASDY NRNIYLDILN YTRQDKELES RYLSLESDSR QMTLVLSLVI
AGLVLVVILW WFFNKRSKIR NQVDVERLQR ILALCRDITS SIPMNVPLIQ QGIDQLFGKG
RLQLEIPEEG KAALVPLHRL NRDEKALVHV LEPYIVWAAD NEQMVEALSD ERMQLEKQRY
VYEQHIAGNK RQNLIKKACL AIVNGINPYI DRILNEVHKL TERGYIDHEK IKKEKYQYID
ELVTTINEYN DILALWIKMK QGTLSLNIET FDLNELFELL GKGRRAFEMK NQKLEIEPTT
VMVKADRALT LFMINTLAEN ARKYTPEGGT IKVYARTTDA YVEISVEDNG RGISEEDMAR
IIGEKVYDSR VIGMKNAADP EVLKENKGSG FGLMNCKGII EKYKKTNELF RGCVFDVESE
LGKGSRFYFR LPSGVRKTMG VLLLCLLLPF GVSSCLHDPI PPMLQEGDSI VVVTDSAYED
LLDAASDYAN AAYFANVDEN YEFALQYIDS AILLLNEHYE KYARPDRSHR YMKLVGEGTP
AEISWWNELF DSDYHVILDI RNEAAVAFLA LKQLDAYSYN NSAFTDLYKL QGEDQTLEAY
CRQLERSNTN KTVGIILCFV LLIVSLVGYY FLYMRKRLQN RLNLEQVLEI NQKVFAASLV
RPQEQENAEA LQREESTLKE IPQRIVDEAF GPVNELLTID RMGIAVYNET THRLEYASRP
GQEMPEMVEQ CFSSGEYLSE QHLQAIPLMV EAGGEHQCVG VLYLERREGT EQETDRLLFE
LVARYVAIVV FNAVVKLATK YRDIESAHEE TRRASWEDSM LHVQNMVLDN CLSTIKHETI
YYPNKIKQIV GRLNTQKLSE TEEREAVETM TELIEYYKGI FTILSSCASR QLEEVTFRRT
VIPVQELLDA AGKYFKKSMK NRSERIELEI EPMEAKVIGD VNQLRFLLEN LIDEALTVRE
DGLIRLQARQ DNEYIRFLFT DTRREKSVEE LNQLFYPNLA RMTSGEKGEL RGTEYLICKQ
IIRDHDEFAG RRGCRINAEP AEGGGFTVYF TIPRR
//
