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Database: UniProt
Entry: A0A2U1AHX6_9BACT
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ID   A0A2U1AHX6_9BACT        Unreviewed;       620 AA.
AC   A0A2U1AHX6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C8D82_1387 {ECO:0000313|EMBL:PVY36007.1};
OS   Victivallis vadensis.
OC   Bacteria; Lentisphaerota; Lentisphaeria; Victivallales; Victivallaceae;
OC   Victivallis.
OX   NCBI_TaxID=172901 {ECO:0000313|EMBL:PVY36007.1, ECO:0000313|Proteomes:UP000245959};
RN   [1] {ECO:0000313|EMBL:PVY36007.1, ECO:0000313|Proteomes:UP000245959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14823 {ECO:0000313|EMBL:PVY36007.1,
RC   ECO:0000313|Proteomes:UP000245959};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-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:PVY36007.1}.
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DR   EMBL; QEKH01000038; PVY36007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1AHX6; -.
DR   Proteomes; UP000245959; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PVY36007.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245959};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        182..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          202..254
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          391..607
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   620 AA;  69263 MW;  4754B77F0F5FD226 CRC64;
     MLDIRKKFLI SFGVLVVLIA TVGAVMMRQV DRLGAAIDVI LRENYRSVVI CRKVDDILEE
     VNGGLLRSFR DGTAEENGDW KEAVRELRAA WDAELRNVTV KGELERAERV NRLLKEYIAL
     LPELAQPRKA ETERRTLYDE RMEPLFREIK ELTGEIQALN QQNMIDANNR ARQEAETLHR
     RVLMILIGCC LFAVILTLLL KNWILNPIAR LLALTNEISN GNLDIVLDAK SGDEIGQLSR
     SFNAMAAALR EARRNERIKL ERSERTNRDV FSELPTPIAV FDARSGRVEI ATRSAEQYFG
     FRIGAEVGAV NAVWLREIYD RVLAGGGVCT CRQNDGVIQH FIDNKEYFFQ PTALPIPADA
     PADRISAVAV ILKDVTMAHE QQELKRSVIS TVSHQLKTPL TSLRMSIYLL LDEKIGPLNP
     GQLDLVMSMR DDGDRLADIM SDLLDLNRVS GRNNLQLEPR RPADLIRAAE ERFRAKCLDR
     EIRLETQVAP DVPDVLVAVN RIDYVFDNLI GNALRFTPAG GSITVSAVRR EDAVEFTVRD
     TGCGMPPEVQ AHLFEQFYRA PGQEPNSGVG LGLSIAKEIV TALGGSIRVE SAAGQGSSFI
     FSIPVTGAKE NQEKNSAQWV
//
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