ID A0A3B7MK07_9BACT Unreviewed; 1390 AA.
AC A0A3B7MK07;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D3H65_06160 {ECO:0000313|EMBL:AXY73589.1};
OS Paraflavitalea soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Paraflavitalea.
OX NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY73589.1, ECO:0000313|Proteomes:UP000263900};
RN [1] {ECO:0000313|EMBL:AXY73589.1, ECO:0000313|Proteomes:UP000263900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY73589.1,
RC ECO:0000313|Proteomes:UP000263900};
RA Weon H.-Y., Heo J., Kwon S.-W.;
RT "Genome sequencing of strain 6GH32-13.";
RL Submitted (SEP-2018) 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; CP032157; AXY73589.1; -; Genomic_DNA.
DR KEGG; pseg:D3H65_06160; -.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000263900; 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; cd00075; HATPase; 1.
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; 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; 6.
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 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000263900};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 781..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 856..1074
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1125..1240
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1272..1371
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT COILED 807..848
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1173
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1390 AA; 157589 MW; BCF52D2A6D8EAD7A CRC64;
MHTGRRSCLS FSLPAWIAIL LCMVTGRAAA HEGLPLSYLG IEQGLSNNAV RSIFQDHRGF
MWFGTFDGLN RYDGYGFQVF RNTFHDTGSL ADNLVHTINE DRDGNIWAGT NQGVSIYAAA
TGRFSPLRYK PYGAPAIRIL NTETKDIQRT RAGDMLVASL IDGLLIAPQG YATAWQVPLV
INDTIYTNYA AGTIRIDDQQ QVWVFVISKG LCRYDAASRQ LRLVNGSLKA AFSFLPDGSQ
FWVGTNNGIF TYDTRTNTYA RALNQYDAEL ATDKVAGFAI DRQRRLWMVT KGNGVKFYDP
ATRQVTHLVA DGRLNSISNE NFNTVVEDRE GRIWLGSHRG GINIIDRQKD RFTTIAHDPL
DANSLVNNYV SAFYEMSDGR IWVGSEFGGL SLWDRRNNQF TNFKYNASHP EGISNNFITS
IREDHTGQVW IATYWGGINR FNRSNNTFTR YKCLNPAFGN QENKMVYQLL VDKEGILWAT
TLQEGGMKGA LYRYNKAADR FEAFDTRLSE LFVLTEDSQG ALWSGNLSQL IRIDRQSRQH
EYYTLGNTIR SIVEDAQGNL WVGTEGGGLV LFDRTTKSIV ARYTMAEGLC NNAVLNILPD
GKGNLWISTF NGVSRFHIAT KTFQNYYQGD GLQSNQFNPN TCLALRSGEL MFGGIKGFNI
FHPEKILSTA RPAQVFLTGI TVDNKPVPFT EQIKVPYSQA VFSFQYVVPE YSTPGKISYA
YYMEGWDRGW NYTGNLRTAS YTHLNEGHYV FRVKSTNTDG VWNPEEVVLH ITVLPPWYRT
WLAYFLYAAV VVSLIYTWWR YRSRQTRLKY EVAIAHLDAE NKRAELELER AEREKEQVLN
EQERAMQEKK LTFFTNISHE FRTPLTLIIN PVKDLLSRQQ EEPQKTDGDL QTVYRNARRM
LSLVDQLLLF RKAESGHDRI RPGRQDVCAL AHDVYLCFVQ QAKAKKISYE FTCSNEQLEV
YADREKLEII LYNLLSNALK YTPDGGHIVL MVGETAGEIV IRVQDNGIGI GEDAGEQLFE
KFYRASGKML TTQKGFGIGL YLVKHFTAQH KGRIAYESKE GEGTVFTLHL LKGQQHFDAG
TIIEQEPAQA ALLEELALED ALSGQAASTE QPDGPLEAVV SEKKSILLID DDDQLLQYLT
TLFKNTYQVY LASDGEDGLK LARKHLPDLI VSDVQMQGMS GIDLCSHIKE DASLQHIPVI
LLTASTSSEV KLKGVEGGAD DYITKPFDKD ILVARVASLL KARTILQHYF YNAITLNNTD
QKISQEYKEF LERCIAIVEN NLENEDFNLK MLLAEIGMSR SNLFRKVKLV SGLSIKSFIR
FIRLRKAAEL FINTNYNVGE TAFRVGIYDI KFFRAEFNKV FGINPSEYIK KYRKAFGSQY
QVNLKDPPPK
//
