ID A0A3G3GP81_9BACT Unreviewed; 919 AA.
AC A0A3G3GP81;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DTQ70_14285 {ECO:0000313|EMBL:AYQ33255.1};
OS Runella sp. SP2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; Runella.
OX NCBI_TaxID=2268026 {ECO:0000313|EMBL:AYQ33255.1, ECO:0000313|Proteomes:UP000270973};
RN [1] {ECO:0000313|EMBL:AYQ33255.1, ECO:0000313|Proteomes:UP000270973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:AYQ33255.1,
RC ECO:0000313|Proteomes:UP000270973};
RA Jin H.M.;
RT "Genome sequence of Runella sp. SP1.";
RL Submitted (JUL-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; CP031030; AYQ33255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3GP81; -.
DR KEGG; rup:DTQ70_14285; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000270973; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 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 InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF00072; Response_reg; 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; 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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000270973};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..919
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017978701"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..633
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 669..784
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 818..917
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 919 AA; 105957 MW; 299040E1D48A9D8E CRC64;
MKGLFFCYLF LIGVWANAQD VLLDPKKDEI DASSRVGIVE DKLSSWSFEQ IQERLFTQNK
SKHILIPFSN HTFWIKCKLK NATAEPQKWV VRWENPLTER IDFYVQATPN GRFVRFEKGS
FREKHHSYIF ENTPSLTLSF APHQTQTLYL KVVNKRGIFS RLVLLPTDAL ERTKYSSIQR
WSILDGSLLI RLIYTSILAL FVIKDLSFKR YSAFIFIRTF SFWGMIGVLG GWLTTYPYWA
TIANNVAIFM SPIGYTFAIR SVVDIRSFPS YVVYLLRVVL GLTVVFALLI LFDYQWYWLK
GAVFLNLGSQ YVLLGIIAVA SYRRFRINWS YGVPLLLGVA SYSLVLTRLL GGLQWAGLFE
LALLFFVLEL LFFGLYLGRI IRTYEEEQLT IKKELYFKKI QTNQLQELDE LKTNFFVNIS
HELRTPLTLI GGYMEDLRRQ NPQNQVYEIV SRNAQRLLVL INQLLDLSKL EAGQLQVTLT
PLRLDTYLKT LFSAYQSLAE SKKIRFTFYQ SQEKVVGEVD QDKLEKIITN LLSNAFKFTD
AGKRVEVGVE YALLNNRLII SVKDEGVGIP NDKLAQIFNR FYQVERPNYA KYEGTGVGLA
LVKELVNALN GTIQVQSKEG KGSVFRVELP VTYKDDVSIG GEYPQAPMNW ASVEIKTEET
NPKHDVDLRL LVVDDNADIR QYVRSIFAKD YWVVEAENGK IGVEKALEMT PDIIISDLMM
PEMDGFEFCK RLKSDEKTSH IPIIMLSAKA NSESRIESWE LGADDYLLKP FQSEEVRVRV
QTLLEKQARL RTYFSAAVGT EKPATDTEEA SKERGFLLKL YALVEQRMSD SEFTAELCAK
EMGMSQSQLL RKLKALTNQT INEYIRDFRL QRAADLLSQN ETTVSEIVYE VGFTNLSYFT
KMFKEKYGKL PSEFFTQEE
//
