ID I8XRB2_9BACE Unreviewed; 1349 AA.
AC I8XRB2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1068_00615 {ECO:0000313|EMBL:EIY53445.1};
OS Bacteroides nordii CL02T12C05.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY53445.1, ECO:0000313|Proteomes:UP000003089};
RN [1] {ECO:0000313|EMBL:EIY53445.1, ECO:0000313|Proteomes:UP000003089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY53445.1,
RC ECO:0000313|Proteomes:UP000003089};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides nordii CL02T12C05.";
RL Submitted (FEB-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:EIY53445.1}.
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; AGXS01000011; EIY53445.1; -; Genomic_DNA.
DR RefSeq; WP_007483503.1; NZ_JH724314.1.
DR STRING; 997884.HMPREF1068_00615; -.
DR PATRIC; fig|997884.3.peg.625; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000003089; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; 4.
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; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003089}.
FT DOMAIN 832..1052
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1093..1208
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1242..1341
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1141
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1349 AA; 155998 MW; E61A09BD02FDB450 CRC64;
MQKVLYLLTL LLITVYTYAD VSPVVINRLT NNEGLSNSSV NVIYQDSNNL MWFGTWDGLN
LYNSREFKTF KPNPNVPGNI TNNIIRDIIE TTKGRLWITT DNGINLYTPE AMRFQSFFYD
NKENSIFKER SFLICKNSHN KVIASVYNTG LYYFDEELSD FILIRNLKET SLKKLFFDKD
DNLWLFTDNN SLYRVNLDWS KNKPDIKDIK PVILSQSSHD VFYNLYTNQI WEQNENRHIN
IYDVPTETKI TEIPFSKVIS SIIFEKTGYV IGTANGLFSI QAQNHEITTL IEDIPVFSIY
KGTQDILWVG TDGQGVIMLT PKNNRFTSYS LKNSSIYGLS PVRCFWENQN KQLFIGTKGS
GLYIFQDDTT ENLFAQFTTN NGLINNSVYA LAGKENDICW IGTDGKGLNY WDYKTKKLYT
LKMNEKLDII SVYAIYIQND HTLWIGTNGF GLYKLTIDRS KTPYEVTEYK QFIYQDHNKK
GLSNNVIFSI IPDDHNGLWI GTRGGGLNHL DTHTYTFTTY RFSEKEMSSI SNNDIITLYK
DPDHQLWIGT SLGLNLMQKD EKETISFKHY TEKDGMPNNT IHGIQADNDG NIWISTNKGL
GKLSKNNDKI ISYYQNDGLQ NNEFSDGASY KSSYTNNLFF GGINGYNKFD PQSIPETTFS
PRLNFDDFLI NNENADIRKF TKKINGKKMI VLNHTENLIG FKFTPIDYIS GMKCEIEYKL
APYEKNWIQM GTSQLIVLNK LPSDDYILKI RFNNANKIWS EDIYEIPIRI LPPWWLSKWA
YLFYFLTSIS ILFVIYSVVK NRIQMKHTLE LSNLEKTKTE EIHQAKLRFF TNIAHEFSNS
LTLILVPSEQ LLKIRNMEPE AKRYVRTIHS NAGRMQKLIQ ELIEFRKAET GFLELQTEIV
DIHEFVKYIT DYFTNTAAQK NIQFSIQIQD DTNTWITDRS CFEKIVFNII SNAFKYTPIN
GYIHLSISQI NEHLILQIKN NGKGIKKEDI HLIFNRFKIL DQFEKQMAQG ENRNGIGLAL
CKALTDLLKG TIEVESELND YTQFTISLPA LELTNKQPVS MPPLVTEEPP INTEYTDITE
LADTDTNNMS QTVILIVEDD KEISNLLYGL LKHKYSLLFA SNGKEGVEMV EKNSIHLIIS
DIIMPEMNGI EFVNHLKGKS TTANIPVIFL SSRTSIDNQI EGLQTGADAY VGKPFNSMLL
ETTIDRLLTS RRSLKDFYAS PLSAIEKIEG KTVHKEEKEF ILKLTRIVSE NIDNENLSIE
MLSNEMGISK IMLYRKLKEI KEETPTEFIR KIRMNQVEKL LKMTNKTIQE IMFDCGFNNK
AYFYHEFSKQ FNLTPGEYRK KHGSKAMNE
//