ID   Q55693_SYNY3            Unreviewed;      1178 AA.
AC   Q55693;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=slr0222 {ECO:0000313|EMBL:BAA10222.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA10222.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA10222.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; BA000022; BAA10222.1; -; Genomic_DNA.
DR   PIR; S76370; S76370.
DR   AlphaFoldDB; Q55693; -.
DR   IntAct; Q55693; 3.
DR   STRING; 1148.gene:10499721; -.
DR   PaxDb; 1148-1001594; -.
DR   EnsemblBacteria; BAA10222; BAA10222; BAA10222.
DR   KEGG; syn:slr0222; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   InParanoid; Q55693; -.
DR   PhylomeDB; Q55693; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 6.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 7.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 5.
DR   PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 3.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 5.
DR   SMART; SM00091; PAS; 6.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 5.
DR   PROSITE; PS50112; PAS; 5.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAA10222.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425};
KW   Transferase {ECO:0000313|EMBL:BAA10222.1}.
FT   DOMAIN          8..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          157..199
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          276..320
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          327..377
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          378..419
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          456..509
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          549..605
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          624..674
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          755..805
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          806..863
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          874..928
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          946..1163
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          500..531
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1178 AA;  134970 MW;  32D09905E07C8453 CRC64;
     MPIIPSPKVL LVDDQRENLV ALSRALDSLP VEIITANSGQ EAIATAATTE FALMILAQEM
     SELDGLNTAK ILRSFPLAEQ TPIIFLARQE IITKAMAEIN ILGLVDFLAQ PPNQNFLQVK
     AKLYLQLFQQ KQTLQYYNNY LESSVKSVHF DVKNNHSEQL SEIILANISD TVFVTDLSGK
     FTFICSNIDN IFGYSLAEVN AMGTVETLLG DFRFNEYELK EKGELKNLRH DVQDKQGKIH
     YLLINLKKVA INGGIYLYSC RDISEWARKE QAIRNSEANF RDIFASIKDG LLVLDEDNYI
     CYANAQAVKL LNCTLEELVG TIGSPLEDTE FSLLVDDGTI YTVDVSVTEI TWYGQTAKLV
     SLRDISDRKR MENQLRENQN KYYRLLENLD NGVIVHNANA EIVYANPKAE SFLGLTDLEG
     RDIDDEYWMF FDKEGEKLEK EEFPVAQVLA NQSSLKNFEM GIYRPDTDQL LWAYINAYPE
     FYNEDTIQEI IVTFSDITER KLAEIQLKTI NENLEVLIEE RTSELESSNS QLLQEIIEKE
     QVSITLTTQE AKYRALVRDA GDAIILITID FIVLEVNYRA VELSGYDQEE LIGHSLLDLR
     LLTPEFYAQQ RHFWRTLKRE QISQLTDVRL VKKSGELISV DISASVITYE NHSIVQCIVH
     DITLQKTIQA QLQRENYFRR QLLEKMVEGL FVCYEVEQFP FLQFTVWNPM MKNITGYSQE
     EINQCGWYET LYSHGQPQEA VRVRMKAVAL GVDMVKEEWQ IIRRDGALRT VEISTALITS
     NNQTNILAVI QDITDQKRQL QIIQNNEATL RCIVENLPIF FGMRTINFSN WYYINPSFES
     LTGYTPDEMY EDPLLWQKIH REEYAENLEQ ARPNLGEWTI FSMEKKDGTQ IWAQTVEFLV
     DDLSDTARVV VFGQDITDIK RAEIETLRSL VKERELNEAK SQFVDIVSHE FRTPLTSIIG
     FGELLSKYFD RLSTEKKQQY INNIQNSSQR LKQLIDDVLS ISRYDANKIE IELGNINLRN
     LANDLIENFS CGLGSEHNFE LNYHLKPDEH SLVDVRLLRH ILENILSNAI KYSAPGSTIT
     LDISKDEEHL LFQVRDEGIG IPLQDQEKLF EAFHRASNVG DIPGTGLGLS IVKRYVEFQG
     GTIEVISMPG KGTTMVIKLP LNPAPIIQIA QGETDRLS
//