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Database: UniProt
Entry: D7K3T7_9BACE
LinkDB: D7K3T7_9BACE
Original site: D7K3T7_9BACE 
ID   D7K3T7_9BACE            Unreviewed;      1338 AA.
AC   D7K3T7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF9010_04429 {ECO:0000313|EMBL:EFI38914.1};
OS   Bacteroides sp. 3_1_23.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=457390 {ECO:0000313|EMBL:EFI38914.1, ECO:0000313|Proteomes:UP000003808};
RN   [1] {ECO:0000313|EMBL:EFI38914.1, ECO:0000313|Proteomes:UP000003808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_23 {ECO:0000313|EMBL:EFI38914.1,
RC   ECO:0000313|Proteomes:UP000003808};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA   Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 3_1_23.";
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};
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DR   EMBL; GG774950; EFI38914.1; -; Genomic_DNA.
DR   RefSeq; WP_008649250.1; NZ_GG774950.1.
DR   HOGENOM; CLU_000445_28_1_10; -.
DR   Proteomes; UP000003808; 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; cd00075; HATPase; 1.
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; 2.
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; 2.
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:EFI38914.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:EFI38914.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1338
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003100358"
FT   TRANSMEM        782..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          835..1049
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1082..1197
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1233..1331
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1130
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1338 AA;  151590 MW;  B41869BC3E9CCAE2 CRC64;
     MKLTKILICL LIFWTGTLSA SPYFSFKKYQ VEDGLSHNTV WCALQDSYGF IWLGTSDGLN
     RYDGRGNKVY RNVLNEKFSL ENNFVEALIE VDKNLWVGTN SGLYIYDRDT DRFSYFDKTT
     QYNVYISSEI KKIIKTENGL IWIATLGQGF FIYDPKTEVL TQNSVQTSFV WDLCQSADRK
     RVYISSLQEG LLCFDENGKF LRTYEISLDI NASDSYKVNC IQNIDGDIWI GAGSNLLSRL
     DERTEAIDNY SGSAFNFGAV HCLLKYTDKE LLVGTDNGLY LFDQNTNTFQ RADNPADPRS
     LSDQTINGMM WDAEGALWVL TNLGGINYMS KQTKRFDYYS PAYLSGVPGA GEVVAPFCEN
     KDGNIWIGTQ SGLYFFNAVT RELSPYAIGG AKNQKYDIRS LMLDGDYLWI GTYAGGIRVI
     NLRTGAVKAY THSRGIPNTI CSNDVLCIYK GRKGEIYVGT SWGLCRYDAA RDNFMTITSV
     GSMVSVVDIY EDMYNHLWIA TSNSGVFSYN TMNAHWKHYQ HEREDSTTIT SNSVITLFED
     AKGTMWFGTN GGGLCSFDAK EKRFIEFDPH NTLLLNKVIY AIEQDQGGDF WVSSNAGIFK
     INPVTKDYFR QFTINDGLQG NQFIARSSLK SSEGKLYFGG INGFNVFQPE QFVDNKYIPP
     VYVTDIRLPY QTDEQEVKKL LQLDKPLYMA DKVTLSYENN SFSIRFVALS FEDPGKNRYS
     YILRGVDKEW ILNTDNNMAS YTNLPPGEYL FEVRGSNNDR QWNENTTTLK VVITPPWWRS
     TFAYVIYVLM LLGWIGWMAW RWNLRVKRKY KRRMEKYQTA KEQEVYKSKI SFFINLVHEI
     RTPLSLIRLP LEKLLEKERE GKELKYLSVI DKNVNYLLGI TNELLDFQKM ESGTLHLNLK
     KSDIKELVSD VYNQFTSPAE LKGIDLQLTV PEQELVSTVD SDKLSKILVN LMGNAIKYAH
     AHIDLRLLVT DGGYEIQVND DGPGIPNEQK QKIFEAFYQL PDDKVATAVG TGIGLAFAKS
     LAEAHQGDLR LEDNIGGGSS FILSLPFKEW ETEKMSDIVE ISPEHADASE TVSSEYSGKK
     FTVLLVEDNV DLLNLTRESL AEWFRVLRAS NGREALEVLA KENVDVIVSD VMMPEMDGLE
     LCSKVKSEIS YSHIPVILLT AKTTLESKVE GLECGADVYV EKPFSVKQLR MQIENLLKLR
     QSFHKLMVSL AGDTVAVSTT DFAMSQKDCE FIAKIQGVIA EQLADENFSI DTLAEQMNMS
     RSNFYRKIKA LSGMSPNDYL KTLRMNRAAE LIVSGTRISE VAAQVGFTSS SYFAKCFKAQ
     YGVLPKEYTG QPPISGEA
//
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