ID C3Q9G7_9BACE Unreviewed; 1356 AA.
AC C3Q9G7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BSAG_00311 {ECO:0000313|EMBL:EEO48601.1};
OS Bacteroides sp. D1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO48601.1, ECO:0000313|Proteomes:UP000003361};
RN [1] {ECO:0000313|EMBL:EEO48601.1, ECO:0000313|Proteomes:UP000003361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:EEO48601.1,
RC ECO:0000313|Proteomes:UP000003361};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. D1.";
RL Submitted (MAY-2011) 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:EEO48601.1}.
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DR EMBL; ACAB02000088; EEO48601.1; -; Genomic_DNA.
DR RefSeq; WP_004313809.1; NZ_JH114344.1.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000003361; 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 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; 3.
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; 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; 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; SSF63829; Calcium-dependent phosphotriesterase; 2.
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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EEO48601.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EEO48601.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 784..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 837..1057
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1097..1212
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1246..1345
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1145
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1356 AA; 156948 MW; 4465113016802B74 CRC64;
MGKTYLSRFF FFLVIGWWSL LDVEATAYSL RQFSSKNGLS NSAILSICQD CDGLIWIGSC
DGLNVFDGTE LRLYKPVDVR NNLSGNLIDN IMEAEDHVLW IQTNYGLDRF DTHLQTVQRF
KDFQDISCMA KTRENDVLVI KDDGYIYYFD RKGLKFHRLN AKRLAFEDIQ YICVDSANVL
WIFSSSGDVR SYVIEKKEDS IPELILQSLF EQEGELFWTS GEGDLVYFID GAYDLYEYDL
RSRNKYFIAD LKEEIAQRGQ VSSIVKQRDD YYVGFKSSGL ICLKYQSDSK VKYVMQSIGI
ESGIFCLFKD RFQDIIWVGT DGQGVYMYFI DHFSIRNTLL DTSDYQINTP VRALFLDDEQ
TLWVGTKGDG ILRMLRYAPD TGGKFDVERL HTGNSSLTDN SVYCFAPSCW NRLWIGTEHG
MNYYSYRERK VKEFPVMVDG KTLRYVHSIC ELNDSTIWVA TVGEGIVKIV LNVSDGEPKV
MFTRRIVLDG GRRASNYFFT SHQENDSILW FGNRGYGAYR MNVKTEVMMP FRFDQEVSNQ
AVNDIFAILS NKKGYWLGTS FGLTHMQSPG NYRVYNEADG FPNNTVHGIL EDGEHNLWLS
TNQGVVRFNI EANTVQAYNR QNNLEVTEFS DGAFFKDERT GTLFFGGTNG FITINENDLT
AMEYMPKLQF YRLSIFGKEY NIYHFLRQDK DVEVLELDYS QNFFNLSFVA VDYINGNNYT
YSYMIDGLSN NWIENGSSTT AVFSNLPPGQ YTLWVKCRSN IMGKESKPYS LVIRIAPPWY
MTQLAYWGYF LLFLLLLWGL VYMAIRRYRR KRDIIIEKLN RQKRDEIYES KLRFFTNITH
EFCTPLTLIS GPCEKILSYA GTDGYIRKYA DLVQQNAQKL NSLIQELIEF RRLETGHKVL
DIQEVAVDEH TRGIAESFGE WVESRKVDYQ LNIEEGDRWN TDVSCLSKIV NNLISNAFKY
TSDGGKITVE QCIEGERLCI RVSNSGKGIK KENLDKIFDR YKILDDFETQ NKNEAFPRNG
LGLAICHSMV NLLAGEIRVM SIPEEVTTFE VVLPMLTVTD AKSGELKELK KQVMPISDKP
VEQKKDIVAD YDASRQTIMI IDDDPSMLWF VTEIFAGKYN VQPFNSAQEA LEQLKLKQPD
LILSDVMMPD MDGRAFAKIV KEDKLLSHIP LVLLSALNYI DEQVKGIESG AEAYVTKPFN
VEYLEKIVER QIRRKEDMKE YYSSIYSAFK LEDGHLLHKE DKSFFEKMMR VIDEYVENPE
LSVELLSASL GCSTRQFYRK LKNVTDKTPA DIIKEYRLTV AERLLLTTNL TVEEIMNKAG
YTNRGTFYKV FSQKFGMPPR QYREMKKKDL KEKDFH
//
