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
//