ID R6CLF8_9BACE Unreviewed; 1461 AA.
AC R6CLF8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN697_02609 {ECO:0000313|EMBL:CDA76460.1};
OS Bacteroides sp. CAG:530.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262741 {ECO:0000313|EMBL:CDA76460.1, ECO:0000313|Proteomes:UP000018392};
RN [1] {ECO:0000313|EMBL:CDA76460.1, ECO:0000313|Proteomes:UP000018392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:530 {ECO:0000313|Proteomes:UP000018392};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CDA76460.1}.
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DR EMBL; CBCL010000104; CDA76460.1; -; Genomic_DNA.
DR Proteomes; UP000018392; 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 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; 4.
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; 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; 3.
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; 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:CDA76460.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000018392};
KW Transferase {ECO:0000313|EMBL:CDA76460.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 893..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 939..1156
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1200..1315
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1359..1458
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1332..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1248
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1461 AA; 167016 MW; 22EA7536DD6094F1 CRC64;
MKRNVVLTII LFLSVIGVRA QLNCTFTHYT QENGLSQNTI MDMIQDSDGL IWFATWNGIN
RFDGYEFKIY KAHKDNDSQW SSNRVEKLEM DSHGNIWCVS YDGRAFRFDK RQEAFHEIKP
QGNIDFIADR IVALKNSSVW LLSPENGAVR VTGNSVTFEN YGKVNNVFLD SRQHEWVLTD
DGLRCIDAKT NKQSTYFATN KKTKAVDKQN FLSAVEADEK IYFGSDKGRI WVNDIKTGEF
TMHTIDANDE VFYMESLKNG KLLIVTRQNG IAITDKKLEK TEWLLTAKSF DFNRYPVLAV
RPDHIGNTWI GVKKVGCVIR VAPEKKEFTV EQLEVEQDAA DRSNPVFCIA SSNNGNVWVH
PEGGGLSIFN PFTKRLEPFF NSIRTPQLRF STKLHSMMVD RQGNLWLGTH SKGLEKVTFF
FNEFNLTQPK DCNDDTNANK VRAIFEDSKK RIWAGTRDGK ISIYEAGTLK PLGYLSTQGQ
ITRQGTPFIG SAYKIIEDSK GTIWIATKGK GVIRLTAEGN SYRMDSFVSN PNDVYSLSHN
SVYDICEDGK GRLWFVTFGG GIDLLEPTAN GSCRFINAHN NLKGYPMERC LKARRMLRDA
QGRLWVGTSN GLLSFDENFS RPESIAFHLY TASNSPETLS SNDIYDILQT KDNRLFFATF
GGGLNELKQS KGNQTEASFI KYGIQDGLPS DVLISMAADN KNNLWIASES GLCKFGLKEH
YFENYLKQEL GSEINFEEST ATSGRDGTLY FGSNRGIVSF KTDNISKSAN VPPIFLARLK
VMNEEILPTE NGILQKSLNE IESISLSHRQ NTISITYATL DMSFPENVRY AFKLEGFDKD
WNYVDWQRSA TYTNLPKGNY VFRVKSTNGA GIWVENEHDL RITVRPLFWE TPWAYLLFVI
GFLTILLIGT YILFIIYRLK HEVSVEQKLT DMKLRFFTNI SHELRTPLTL IDGPVNFILR
RSDLNDEVRE SLKVVERNTQ RMLRLVNQIL DFRKIQNNKM KLRVEHVEIV SFTQRIMENF
QTIAEENRID FLFETEKSQL YLWIDADKVE KIIFNLLSNA FKYTHPGKNI KLFIHEDENT
VSIGVQDQGI GISENKRKSL FVRFETLLDR NLFAQNSSGI GLSLVKELVD MHHATIDVES
KEGEGSCFTV HFKKGKEHYD DNVEFVVADD IYVTNGNEEP AATTETTTAE SEAQADDQQT
MLLVEDNVEM RFFLRSIFAK RFKVIEASNG NEGLEKATTF IPDIIISDVM MPEKDGIQMT
RELRNQLATS HIPIVLLTAK TDMDSKLQGM ELGVDSYITK PFSAVYLEAR VNNLLERRRS
LRQFYYEHLM DSTPAGQPEP AEAQEQTQAM SPQDRKFIDK LTELMEKNMD NGDLVVDDLV
KEMAVSRSVF FKKLKSLTGL APVEFIKEMR VKRAANLIES GEFNMTQIAY MVGINDPRYF
SKCFKQRFGM TPTEYKDRNK K
//
