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
//
