ID A0A286IQH2_9BACT Unreviewed; 1376 AA.
AC A0A286IQH2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN06298216_3299 {ECO:0000313|EMBL:SOE22898.1};
OS Spirosomataceae bacterium TFI 002.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE22898.1, ECO:0000313|Proteomes:UP000217493};
RN [1] {ECO:0000313|EMBL:SOE22898.1, ECO:0000313|Proteomes:UP000217493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFI 002 {ECO:0000313|EMBL:SOE22898.1,
RC ECO:0000313|Proteomes:UP000217493};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; LT907983; SOE22898.1; -; Genomic_DNA.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000217493; Chromosome i.
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; 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; 2.
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; 2.
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; SSF101898; NHL repeat; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000217493}.
FT DOMAIN 852..1077
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1122..1237
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1269..1368
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1170
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1376 AA; 157178 MW; A92B3CD2F3FF1E1E CRC64;
MLKLIIYSTL AMTRELKKFY SVLITCTLVL NTSILFSQSS TYRFKNFTTD IGLSHHHVTC
SQEDKTGFMW VGTVEGLNRF DGYNFRPYFH SENDSTSISS NRIQTLILDE KGRLIVGTNN
GLDIYNEINN TFSKIPLRTK KGDFTDATIN DINKDAEGNM WVSSNSGLFV LGKDKKVIEH
YTKGILQGNE IGHLLIDKNQ NVWIGEPKVI SKLNIKTGKI TRFPLTERFK IDRDPPVNAI
IQDSKGRIWF SSNQAGFSLF NEKLQKFEYY PLASISPNDV LRNRVRAIKE DEQGRLWLGT
FDGLIIFDPE TKYEIKIVKD HNNPYSISDN GITSIDSDSN GNYWIGLYYG GISYFDKNFN
IFNHYQHTGD NKGLSYNVIS FISQSDDGKI WIATDRGGLN LFDTKTQTFK FFNQQDNPSG
SASNHIMEIE IGKNDNIWLG TLYGGVYSFD RKTHSFSPLK FVKNEPEDLG FKRIRGLKLD
QKGNLWIAHV MGLHYYDVSQ GKTLKYASEL NDVKLQNAIN AIFEDSKNTI WLALNQPEGL
VKLEDENWEH KKYPIPNVTC IFEEKDYIWL GTSNNGLYRL DTKTESIKNF KSSDFLNKDI
VGILDDEQGN LWLSSSEGLV VFDKKTEKYL DLQRAHGIQN DVFKRRAYLK SKDGKMYFGG
LNGMISFDPQ LINDGVFTPK VEITDIKIGS KKSNNDLGRS LVGKMNSTKT LHLDYDQNTL
FIDFAALNFS QPERTEYAYK LEGFDDWNYI GTDRKATYTN LDPGTYSFMV KATNSNGEWV
SESKAISIVI SQPPWLTWWA YILYGIALSG LYLLAKNIVS NRIRLKNELR LEHFKNEEEK
KLHEMKYRFF TNVSHDLRTP LTLILGPLEK LLQNHQGDNT VRNLYTTAYK NAEHLLKLVN
QLMDFRKLES VHNELEVAQG NIVLFINEIF LSFQEQARIR NIQYTFSSED DNILVFFDRD
KIEKVFYNLL SNAFKFSPDG SEIGINISFE GNQSVEFPAG FLKIVVSDQG IGIPQNEQGT
IFDRYAKSSE SKPMIEMSSG LGLDIAKGFV KLHKGSISVE SEKNKGSKFS VCLPLGSSHL
NKQEIDANFK NSESEVHYQE SEIVSPILTH SVDDKSKAMQ SLILIVEDNL DIQAFLHGIF
NTNYRIITAS NGEDGLEKAI EHCPDLIISD VMMPKMNGIE LCSSLKRDLK TSHIPIILLS
ARTSLIFKVN GLETGADDYV GKPFIPQILE LKVKNLIEGR QVLRERFVKE FNLSPKELAV
NTADERFLQI LIEGIEKNMK NPDFGIEFLG KEVKMTRGHL YRKVKAMTGM TASEFVRLVR
LRYAANLLKN SLLNINEICY EIGFQDPNYY RKCFKKMFGV SPSEYKENPS KYPVLT
//
