ID A0A3B7MYY3_9BACT Unreviewed; 1358 AA.
AC A0A3B7MYY3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D3H65_32525 {ECO:0000313|EMBL:AXY78429.1};
OS Paraflavitalea soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Paraflavitalea.
OX NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY78429.1, ECO:0000313|Proteomes:UP000263900};
RN [1] {ECO:0000313|EMBL:AXY78429.1, ECO:0000313|Proteomes:UP000263900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY78429.1,
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; AXY78429.1; -; Genomic_DNA.
DR KEGG; pseg:D3H65_32525; -.
DR OrthoDB; 1489484at2; -.
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; 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; 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; 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 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:AXY78429.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000263900};
KW Transferase {ECO:0000313|EMBL:AXY78429.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 795..817
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 838..1059
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1098..1213
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1254..1353
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1146
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1358 AA; 153597 MW; 769693BD261C6637 CRC64;
MKLPYMKKYT RPSILYPVLL AALLLAGLLP CMAQQAAFRH LTVEHGLSQN AVIAISQDNL
GFIWIGTPNG LNRYDGYRIK QYQSRPNDST TLSANSVLAL LNDSRKNMWA GTQDGLNRYD
ARLDRFTRIK SPIEKPLAFY VLYEDRKGRI WAGTDYGLFV VDAALPGVLQ PVLLPGQQAI
DQQWNVRTIY QDRNGALWIG ATAGLLLMQE TGASRQFIHF KHQPADPRSI SADFVTSLAE
DRYGKLWVGT HSNGLNLYDA QQKTFSHFLH NNNDPQSIIS NTIRKVLLDK EGHLWVGTQE
GLSILDEAGK LLYSYQQNDA DPGSLSHNSV HSLFQDFTGN MWIGTYFGGA NYAYAVNTRF
SVIRKKDEPG FLNNNVISSI TEDEKKNLWI GTEGGGLNYY DRSTGRFTSY RHNPGDPGSI
GSNLIKVVYR DWQGQIWCGT HGGGLNLFDP VHKKFTRYLY EDNNPAYLNA EIVSIYEDTK
GRLWVGSTMG IKLYDKSPQG LTPVHLPLTS HPVFANTAKY FFEDDKNRLW ISTNSGLFLL
RNDSIQKLSD NIVNCVMQDK YTQVWWGLQQ AGLARFDESS QKPVYLTQPE KISSRNIFGI
LEDNQQNLWL SSDNGLLKFN PPQNQLQLFT VSDGLAGNAF NYNSFFKDSK GAFYFGGFNG
ITWFAPDKIV SNPRAGNTVL TGLKLFNKQI VPGDSTGLLK ENIAGIDHLT LKHNQNVINL
EFALINYIKS NKNSYAYKLQ GYDKDWVYTN TPVASYVNLP SGDYDFIVKG ANNDGVWSNP
IQLPIEVLPP FWNTWWAWII YTLIAIGIIF LLSRYIFLRE LFKKEDELHQ VKLNFFTNVS
HEIRTHLTLI MAPVEKMQES EDTSGFARQQ LDSIHKNANR LLKLVSELMD FRKAETGHLK
LQVAQHDLIP FLEDIYNSFQ DIALKKNIST SFIYDGTQLL LWFDREQLEK VFFNLLSNAV
RFTPENGQIT LQVTETPTEA IIKVMDNGRG IAAEYLDKVF TNFFQVDDHG LQNTGYGIGL
ALAKNIVFLH KGSITAESIP AANDQTGHTT FIVRLFKDNR HFNQVKATDQ PPVPIPAALP
AANPVPNELQ PAAGQQPTLL IVEDNVELRN IIKEKFAGQF HVLEAPDGAK GLQLAVHEIP
DIIISDVMMP QMDGFEFCRH IKTDHRTSHI PVILLTARST QTDHVSGLET GANIYMTKPF
STKVLELNVR NLLLAREQWR RLFMQQLHTA VSPTTPVPVP KEPVVNTIEQ AFLEQVVRIV
EENLDNQEFG VDMLSRKVAM SAPILYKKIK AVSNMSVNDF IKSIRLKRAA ELLREKQLNV
FEVAQAVGYN DRKYFSKEFK KQFGTTPSEY TGEALKDQ
//
