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Database: UniProt
Entry: R7A106_9BACE
LinkDB: R7A106_9BACE
Original site: R7A106_9BACE 
ID   R7A106_9BACE            Unreviewed;      1383 AA.
AC   R7A106;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BN800_01668 {ECO:0000313|EMBL:CDD49274.1};
OS   Bacteroides sp. CAG:875.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262752 {ECO:0000313|EMBL:CDD49274.1, ECO:0000313|Proteomes:UP000018287};
RN   [1] {ECO:0000313|EMBL:CDD49274.1, ECO:0000313|Proteomes:UP000018287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:875 {ECO:0000313|Proteomes:UP000018287};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDD49274.1}.
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DR   EMBL; CBHD010000083; CDD49274.1; -; Genomic_DNA.
DR   Proteomes; UP000018287; Unassembled WGS sequence.
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; 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   SUPFAM; SSF69322; Tricorn protease domain 2; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1383
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004439297"
FT   DOMAIN          844..1064
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1116..1231
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1268..1367
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   REGION          1363..1383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1365..1383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1164
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1383 AA;  156665 MW;  1497B3EBCD5D7533 CRC64;
     MKNYTLILLF LLGLALPSRA QRLLEKDFQV LNMNDGIADN DIHSIEKDAE GFIWFGTSSG
     LSRYDGQDFK TFRITEALHR TVGKVVSLNK DYLLVRSERT LFLFDKQRER FLSLWDAERN
     RIVDFTRFVA TSDGHCWGVA GNTLSEMDLS TASFREDTAF VHLQSTVKVE SESELMMLCL
     GEDGKSLYGI GRKGTVYRYD RGQKRLETLC VRPMQRDVLV TSALQGDNFL WITTLGDGLY
     GYDLTTCAVH HWNYDPANRN EQLSHNDVFQ LLPLGDSRYM ALTWNGYTML TLTPERELKM
     HAFHSFGNSG NQYIETRMVT GYYDPEGLLW IGTEGGGVLF SDLRQLFYQQ YAQAHSNELC
     GIQMDKEGYL WLATFHKGLL RSTQPFDGIQ PLDFQPMAPG VVAIHTVLCS AADTCGGLWF
     GSRNGRVLRY GEDGSWQALG LGKETSPEVW SLLPLSENEA WAGTSNGLYR VNLRKGTSVK
     VEWNNPQIPD HIQVRALALS DARTLWLGTT RGLLRLSMEG NRVVRSCAGY EREADLSPTD
     VEVRALLFGS DHVLWVGYAG NGLGACSPVD NRILFHYTTE DGLCSNFVTA LAEDGDHSLW
     VGSNSGISRL SRHLQSFYNF YISGSNRSVF FGKDFLFWGN HSTLTYFRPS RLRFHYPIEK
     GRVVFTDLEV NHTSVQIGEH VNGQVILSRS LLYTKGIHLN HANRNFSLSF SNLLYLHKLQ
     KYLYRLYPYQ EEWIMADEGD KISYDRLPAG EYTFQVKTVF QDQSEGEVSS LDIVVDPHWS
     ETWWFRLLAT LGLMGILLVY IHRVRLKEKR VQYELRLEHE LFTVNMERNK EIELRKERED
     FFTMAAHELR TPLTLILAPL RELLHKTPTS HPFYAKLSMM FKYAEGLHTL TDRLLYIQKA
     EAGMVKLRLS QVDVEALLVD VAQGFQSLAA ERKIDYAWEL APDCVPVWAD REKLSSVVQN
     LISNAFKYTP EGGKIRLKVE RKEIDGKHFC CLSVSDTGKG IDSVLLQHIF DPFVTGKEAP
     AVSTHVGIGL KIVKHIVEMH HGRVTVDSEP GKGSLFCVYL PEGKSHFNED DCTWEESSEA
     VVAPEVSSVV PEMIFPATSE HVAEAKEEKL SAARQTVLVI EDNTDMRRYL CELLRKQYRV
     LEAENGEEGL KTAVEQVPDL VLSDVMMPVM DGFTCCAELR KRKETAHIPV LMLTAKAEDR
     DSVEASRRGA DDYLRKPFNP EVLLAKIACL LDMRRRLKQI YTRTLLHASS AASASTEKPE
     SVESEFMQKV WACIEANVSN PDFNVKVLSG ELHMSLATLY RKLKQHTDLS AVELIRHIRM
     TKAALLLMET SLSVTEVAER VGFNDLPTFR KHFTDMFGVS PSKYAESGQG GNNKSQPEAG
     TGV
//
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