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Database: UniProt
Entry: A0A1W1X9W2_9NEIS
LinkDB: A0A1W1X9W2_9NEIS
Original site: A0A1W1X9W2_9NEIS 
ID   A0A1W1X9W2_9NEIS        Unreviewed;       451 AA.
AC   A0A1W1X9W2;
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_01033 {ECO:0000313|EMBL:SMC20617.1};
OS   Andreprevotia lacus DSM 23236.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Andreprevotia.
OX   NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC20617.1, ECO:0000313|Proteomes:UP000192761};
RN   [1] {ECO:0000313|EMBL:SMC20617.1, ECO:0000313|Proteomes:UP000192761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC20617.1,
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; FWXD01000004; SMC20617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1X9W2; -.
DR   STRING; 1121001.SAMN02745857_01033; -.
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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SMC20617.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192761};
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   TRANSMEM        152..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          169..224
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          232..446
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   451 AA;  49292 MW;  C21DCADDC29E1394 CRC64;
     MGRLFWKILF GFWLTLIVVT LTVNAVANHY NESRLRASSE VALGGRVAMM TTAAAASLRH
     GGPPALQALF DGWPRFARDR LLVVDAHDRD LFDRPVPPPA LAEARRVLRD GLVDNQSVIS
     VDTPQGEVLF FVLADNMPHR GPPPPRGVPG FMLLWFGVGS LAFSAVLAWY LTRPIRVLKQ
     AFDRVSEGDL SVRVGPRIGS RRDEIADLGR DFDIMTGRLA QLVASQKQLL HDVSHELRSP
     LARLQVAVGL ARQQPEKIAP TLERIEREVH RLDTMVGELL TLSRLEAGAQ QEWDDYFDPI
     ELAEEVVADA TFEAAASEVR IGLLRDATPE EGVVVHGRAE LLHRALENIV RNAVRYSQGG
     QLVSVAVRQP DAAHCVIEVM DQGPGVPEEQ LQRIFEPFIR VGEQSSGYGL GLAIAQRAVQ
     AHGGTIAAAN RPEGGLVITL TLPLVPTGQA A
//
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