ID D6D1A1_9BACE Unreviewed; 1540 AA.
AC D6D1A1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BXY_31960 {ECO:0000313|EMBL:CBK68203.1};
OS Bacteroides xylanisolvens XB1A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK68203.1, ECO:0000313|Proteomes:UP000008795};
RN [1] {ECO:0000313|EMBL:CBK68203.1, ECO:0000313|Proteomes:UP000008795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB1A {ECO:0000313|EMBL:CBK68203.1,
RC ECO:0000313|Proteomes:UP000008795};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Bacteriodes xylanisolvens XB1A.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK68203.1, ECO:0000313|Proteomes:UP000008795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB1A {ECO:0000313|EMBL:CBK68203.1,
RC ECO:0000313|Proteomes:UP000008795};
RA Pajon A.;
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; FP929033; CBK68203.1; -; Genomic_DNA.
DR KEGG; bxy:BXY_31960; -.
DR PATRIC; fig|657309.4.peg.2022; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2207; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000008795; Chromosome.
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 CDD; cd00146; PKD; 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; 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; 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; 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; 3.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 928..949
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 974..1191
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1252..1367
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1438..1537
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1393..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1300
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1540 AA; 176232 MW; 0E57E9CA56BCFDB7 CRC64;
MILQVFFYLY ATEPSDMMKK TLISVILLLA VVFSTYAQQH CFFTHYSTED GLSQNTVMNI
LQDHKDNLWF ATWDGINRFN GYTFKTYKAR QGNYISLTNN RVDRMYEDRY GFLWLLTYDN
RVHRFDPKTE TFEQVPAAGE EGSAFNVHTI EVMPNGTVWL LTENDGAIRI LTHPDENNRL
TWDIYSSKTE LFPSLHVFKV HQDKAGNDWL LTDNGLGMIH PGKKEPDSYF TETKGKFGGM
NQAFYAVQER DKDICFASDH GRIWSYQKES GEFTLIELPT KGQITSIHPI APDVSVITTD
SDGFFTYNLR TKTNAHYSFL TCKALPAKPI LSAYVDRSSE VWFEQEEPGV VAHFNPSTGV
VTREQIPIEY SNPERSRPAF HIHEDVNGYL WVHPYGGGFS YFDPQKKCLV PFYNGLGSRD
WRFSNKIHSA FSDKQGNLWL CTHSKGLEKV TYRNVPFAMM TPMPHEHESL HNEVRALCED
KLGNLWVGLK DGILRIYDAG KTYKGYLTEN GTISTIGTPM LGTVYFVIQD SKGIIWIATK
GDGLVRAEPT SSNGMSYKLT RYLHREDDMY SLSDNNVYCV YEDHYGRIWL ATFAGGINYI
TENEAGKTLF INHRNNLKGY PIDPCYKARF ITSDNNGRLW VGTTTGAVAF DENFKKPEDV
KFYHFSRMPN DTQSLSNNDV HWIISTKKKE LYLATFGGGL NKLVSISKDG HGEFKSYSVL
DGLPSDVLLS IREDSKQNLW ISTENGICKF IPSEERFESY DERSITFPVR FSEAASALTA
KGSMLFGASG GVFIFNPDSI RKSSYIPPIV FSKLTVANED ITPGGNSLLK VDIDDADKLV
LSHQENIFSV HFAALDYTNP QNIQYAYILD GFEKQWTFAD KQRSVTYTNL PKGEYVLRVR
STNSDGVWVD NERILDIVIL PSFWETPIAY VLYILFILII ILVAVYILFT IYRLKHEVSV
EQQISDIKLR FFTNISHELR TPLTLIAGPV EQVLKNDRLP ADAREQLVVV ERNTSRMLRL
VNQILDFRKI QNKKMKMQVQ RVDIVPFVRK VMDNFEAVAE EHRIDFLFQT EKEHLYLWVD
ADKLEKIVFN LLSNAFKYTP NGKMITMFIR EDENTVSIGV QDQGIGIAEN KKKSLFVRFE
NLVDKNLFNQ ASTGIGLSLV KELVEMHKAT ISVDSRLGEG SCFKVDFLKG KEHYDKETEF
ILEDAEAPVR MGQVVDIANS SIQSETLIPD DSEKIEAVYE EDAAKEENSK ELMLLVEDNQ
ELREFLRSIF TPMYRVVEAA DGREGANKAL KYLPDIIISD VMMPEKDGIE MTRELRADMT
TSHIPIILLT AKTTIESKLE GLEYGADDYI TKPFSATYLQ ARVENLLMQR KKLQSFYRDS
LMHINMSVTS GELPASTKAM AEEEKKIVSE REEEQTQLQS QQQPTIPDMS PNDRKFMDKL
VELMEQNMDN GDLVVDDLVR ELAVSRSVFF KKLKTLTGLA PIEFIKEIRI KRATQLIETG
EFNMTQISYM VGINDPRYFS KCFKAQVGMT PTEYKEKIGR
//
