GenomeNet

Database: UniProt
Entry: A0A1K1REP6_9BACL
LinkDB: A0A1K1REP6_9BACL
Original site: A0A1K1REP6_9BACL 
ID   A0A1K1REP6_9BACL        Unreviewed;       698 AA.
AC   A0A1K1REP6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02799630_05978 {ECO:0000313|EMBL:SFW70150.1};
OS   Paenibacillus sp. UNCCL117.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1502764 {ECO:0000313|EMBL:SFW70150.1, ECO:0000313|Proteomes:UP000182480};
RN   [1] {ECO:0000313|EMBL:SFW70150.1, ECO:0000313|Proteomes:UP000182480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNCCL117 {ECO:0000313|EMBL:SFW70150.1,
RC   ECO:0000313|Proteomes:UP000182480};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FPIU01000039; SFW70150.1; -; Genomic_DNA.
DR   RefSeq; WP_072338204.1; NZ_FPIU01000039.1.
DR   AlphaFoldDB; A0A1K1REP6; -.
DR   STRING; 1502764.SAMN02799630_05978; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000182480; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFW70150.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182480};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..698
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009667580"
FT   TRANSMEM        206..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        237..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          466..692
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          436..466
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   698 AA;  77090 MW;  CF610A50F15A2E73 CRC64;
     MRVKVLIRLG LLASLLAAGG FLRPVPAAAA DEPAAAAAVP FSADSTTVTE LSGPWMFYWE
     RLLAPEDFNS LESDPGAAAA VMLPHTWGSS SSGTAPSSKG YGTYRILVNL APEKEHAVQG
     LYIPAAATAY RLWINGELKA ENGKVGTSRA EMVPKNYAKV VYFNARPGVN EVILQVSNFV
     QRKGGLWTEL YIGDAEAVTL MREKNIVAQL VISIALLTLG GYHLALFALR KLDRLSLLIG
     IFCSMLSLRS LLLGDTLFIR FFPGIPWELA VKAEYLAPYW GISIFVLFVC LLYPGELPRK
     AAYALSGTGF LFSLVVLIFP ARIFTYTMFP FQLYLIGIFS YMTYIFALAA YRRRVGALLN
     GVSSLIMFAA ALNDILYYNG LVKTTDFVPY GVMQFIIVQT LIVALKFSKA YYKVEKLSDE
     LLVLNATLED RIKDRTKELE RSYGQLKEAN EHLKHAESSR QRLLANISHE LGTPMTAVQG
     YLKAMLDGVI RPNDRSYLQM IYDKVILVSR LVQDLFDLSK LEAGKASFNF TYVTLEDLFR
     DYVDKYRLDV ENRQLRFELV PPAYEAGIGT PLVYVDVFRM QQVIGNIVFN ALKFTPPGGT
     ITIRGELHIK PDKPQEGVVA ISVSDTGTGI HPSVLNQVFD RFVKGGGSQE GEGSGLGLAI
     VKEIVDIHGG NVEAESQPGE GATFRFTLPV EILPEEVE
//
DBGET integrated database retrieval system