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Database: UniProt
Entry: A0A1W1Y0R2_9NEIS
LinkDB: A0A1W1Y0R2_9NEIS
Original site: A0A1W1Y0R2_9NEIS 
ID   A0A1W1Y0R2_9NEIS        Unreviewed;       526 AA.
AC   A0A1W1Y0R2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-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=SAMN02745857_04065 {ECO:0000313|EMBL:SMC29727.1};
OS   Andreprevotia lacus DSM 23236.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Andreprevotia.
OX   NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC29727.1, ECO:0000313|Proteomes:UP000192761};
RN   [1] {ECO:0000313|EMBL:SMC29727.1, ECO:0000313|Proteomes:UP000192761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC29727.1,
RC   ECO:0000313|Proteomes:UP000192761};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-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; FWXD01000041; SMC29727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1Y0R2; -.
DR   STRING; 1121001.SAMN02745857_04065; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000192761; 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; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF13188; PAS_8; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SMC29727.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192761};
KW   Transferase {ECO:0000313|EMBL:SMC29727.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          201..234
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          316..522
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   526 AA;  58490 MW;  29B1735716EF246A CRC64;
     MPRLHPPPSE LHWRSLALLN VFRFLGLIAL LTSLTLLVRR SPMSADQWPF FLQLCGAYIT
     MALIFAVGIA RRLPVFHVQL GVQVLADVLF IVGIMHLMGG IKSGLGILLL PYLAAAGLIA
     RGRMSLFHAA LASIAILLEQ TWQWLQLRAA LDEFLVPALL CAACFAVAWL AHRLARYAAE
     SERLAEQRGI DLANLAQLNA RILQDVSDGV LVVDRHGTIR QCNDQAVRLI GLQPAADATL
     PAVLPGLDLA LAAWRDNPKQ LPPLLQAMSR KTLRPRFVRL TASYDLEVLV YLEDMDKLRR
     EAQQLKLAAL GRLTANLAHE IRNPLGAISH AGQLLREDCG DSPLQLRLTQ IINENAARLE
     RMVRDVLELN RRDRVQMSEI RLPGWLLTFL DEVRQAEEIT VTVALVCPDE AVVRFDPGHL
     HQVLWNLLRN GWRYCSKGPG SLAVMVSERD GRWRLDVLND GPPVPADAQS QLFEPFFTTE
     SKGTGLGLYI AREICAANAA LLEYIPSGEV GACFRIVFGR YDVQKT
//
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