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Entry: A0A364Y8Z3_9BACT
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ID   A0A364Y8Z3_9BACT        Unreviewed;      1366 AA.
AC   A0A364Y8Z3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DQQ10_07240 {ECO:0000313|EMBL:RAW02320.1};
OS   Pseudochryseolinea flava.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Pseudochryseolinea.
OX   NCBI_TaxID=2059302 {ECO:0000313|EMBL:RAW02320.1, ECO:0000313|Proteomes:UP000251889};
RN   [1] {ECO:0000313|EMBL:RAW02320.1, ECO:0000313|Proteomes:UP000251889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDU1-6 {ECO:0000313|EMBL:RAW02320.1,
RC   ECO:0000313|Proteomes:UP000251889};
RA   Li Y., Wang J.;
RT   "Chryseolinea flavus sp. nov., a member of the phylum Bacteroidetes
RT   isolated from soil.";
RL   Submitted (JUN-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};
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:RAW02320.1}.
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DR   EMBL; QMFY01000002; RAW02320.1; -; Genomic_DNA.
DR   OrthoDB; 9806995at2; -.
DR   Proteomes; UP000251889; 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   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; 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; 4.
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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:RAW02320.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000251889};
KW   Transferase {ECO:0000313|EMBL:RAW02320.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        781..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          838..1060
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1099..1214
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1247..1346
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   REGION          1341..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1147
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1366 AA;  155311 MW;  39007987BA2A286A CRC64;
     MVSIRMLLTV ARIFVFAGLV LIMAFTSASG QQLFFSNLST RDGLPSNVIN SIAQDSNQFI
     WIGTGNGLAR FDGYSFKTFK RNENANSLPA NEISCLLVDG DFLWIGTWRG LCKINTKNFQ
     ITRIDLTFEA AIRTLYKDKD NNIWIGTANG LVKHNDGKFI TFTVENSKLS HNTIRSIYED
     NAGVLWVGTY DGLNTLLPSD LEFKHYDLKR DYKPALKNNL ICDIKPVKGN DSLLWIGTET
     GLCLFNKVQK SYKHFTRENA GFSNEVIKNI YVGPNGELWL GTDFGLNVFT TGSKTNKAYF
     NNPQLRYSIP NNMIWEIFED AGGIIWIVTS NGLSRINKDN RLFSYHEITH RIGDQMVGNQ
     SKAILVSKRG IVWIATIHGV VRIDPRTNTQ KVFNIESPPQ ERLILNNVFA LEEDDNERIW
     IGTAGGINVW DEVHKKMHTI NAGNSTGLTS NYIAKFIKGV DGSFWVSAWE GGLFKLVSDI
     NTLSAAKFEF VGDFASEKIT YALNALWAIH NNQLHRIDLN TFGAKKVHRY NAVATGKDIY
     TLHYAPQGSI WTGAANELIE YKPSLDSATV HPITTGTDIN FNNIISDNFG NIWAASDKFV
     IKYSPTTKDF ELFPLEKDLP LKTFYSNCAA RTFDNQILFG GDNGYISFFA GIKTTPYKPN
     VFITNIDVNN KSIQPLQVLN GNTTLTTDVA FIRELELDYA QRSVTFSFAS LHYWQPEINV
     FAYKLEGQEK EWHYVSGVKN FAVYSNLLPG KYTLKIRGTN NYGIWSDRET SIQVIVNPPL
     FLSPIFIAIY IVLAIVTILV GLRVYVIRLK LKNEIKLTRV EKEHAEELIR AKQQFFTSIS
     HELRTPISLI IPPIQQIIKR NNLDEENKRL ITLAEKNSQR LLRLINQILD FRKLEHENQA
     LKLSWFDLIG FCRELHTLFT DKAARSEITF TFDPEIETCE VWADKEKVEI IIFNLLSNAF
     KFTPKEGKIN FKISVAKSDS PREGYVSIAI SDSGIGIAQE EQSKIFEQFY QVQEARKFEN
     GSGIGLTLVA EYTKLHRGEI KLVSSKDHGS TFVVLLPLGH EHFPVQRDDQ GTEVDVLAKR
     TVESSTTEYE FNLRSSKPII LLAEDNADMI DFIQVTLKEK YNFVIAENGS EALNKVSQFA
     PEIIISDIMM PVMDGLELCR RIKEDNKTRH IPFILLTAKS LTTQKVEGIK MGADIYMTKP
     FEIELLEAHI DHLLERKAEL AQYFKNELIT QPQEKNNKEN EDDRFLKKVM NTIEANISNP
     DFSVELLSDE MGMSSTHLYR KLKSLTHLSA NEIIKKYRIK KASILLKNKE GNISEIMYEV
     GFSNLSYFSK CFKTEIGTTP KEYQQRESKH SYDVSEDLES NDGNAK
//
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