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Database: UniProt
Entry: Q2SJ20_HAHCH
LinkDB: Q2SJ20_HAHCH
Original site: Q2SJ20_HAHCH 
ID   Q2SJ20_HAHCH            Unreviewed;       527 AA.
AC   Q2SJ20;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=HCH_02554 {ECO:0000313|EMBL:ABC29354.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC29354.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC29354.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC29354.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC29354.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2SJ20; -.
DR   STRING; 349521.HCH_02554; -.
DR   KEGG; hch:HCH_02554; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_5_6; -.
DR   Proteomes; UP000000238; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 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; 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   Ion channel {ECO:0000313|EMBL:ABC29354.1};
KW   Ion transport {ECO:0000313|EMBL:ABC29354.1};
KW   Kinase {ECO:0000313|EMBL:ABC29354.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW   Transferase {ECO:0000313|EMBL:ABC29354.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000313|EMBL:ABC29354.1}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          292..508
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          505..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  58003 MW;  4A7E64F60E293827 CRC64;
     MLRNYCVLKD INAHFKPKDF WLATLIMLGA MLASLVITQV LAHPNVLLVL FLGVLAAGVK
     TSVWPALWSA LLGFFAYNYF FTHPHYTLKV THSEDLLTII FFLLVSTISG NLAVRLKEQV
     LAIRESKREV EDLLSLSSKL SLAPDRRSIM EVALKEMAKL VSAPVLAFEK GLVEQGSALD
     ARGEPFALPA SELALARRIW EQSASDSSSA RTSPEQPSQY KWLPVCSEMG VLCLLGVPDG
     AYKALDWELH NRISNLTQQL KLSLLRTKLN EELEEVRFQA ETERLRAALL SSVSHDLKTP
     LAAMIGSAGS LLQYHDRLSD EDRKELMETT LQEAERLDRY IQNLLDMTRL GYGALKLHRD
     WTSLHDIVGA AVKRLVNELK PLKVNIELAP DIPLLYVHAA LLEQALINIL ENAAKFSPEG
     GRIDILASVE STSLIIDVID QGPGIPPEER EQVFNMFYSV TKGDRKPSTG LGLAICHGMI
     GAHGGSVEAL DGKDGRGADI RIILPVDPQP ESDPDGALDG DPAEGAE
//
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