ID   D8G2H6_9CYAN            Unreviewed;       999 AA.
AC   D8G2H6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=OSCI_3190006 {ECO:0000313|EMBL:CBN56816.1};
OS   Kamptonema sp. PCC 6506.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Kamptonema.
OX   NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56816.1, ECO:0000313|Proteomes:UP000004532};
RN   [1] {ECO:0000313|Proteomes:UP000004532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX   PubMed=20675499; DOI=10.1128/JB.00704-10;
RA   Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT   "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT   reveals several gene clusters responsible for the biosynthesis of toxins
RT   and secondary metabolites.";
RL   J. Bacteriol. 192:5264-5265(2010).
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   -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC       family. {ECO:0000256|ARBA:ARBA00006402}.
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DR   EMBL; CACA01000284; CBN56816.1; -; Genomic_DNA.
DR   RefSeq; WP_007356021.1; NZ_CACA01000284.1.
DR   AlphaFoldDB; D8G2H6; -.
DR   OrthoDB; 474548at2; -.
DR   Proteomes; UP000004532; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR013515; Phytochrome_cen-reg.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 3.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 4.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 2.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW   Transferase {ECO:0000313|EMBL:CBN56816.1}.
FT   DOMAIN          32..215
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          525..668
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          725..999
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   999 AA;  112927 MW;  F8D6F73966D42372 CRC64;
     MNLVENTQEL KQRLDREVLL RRITKRIRQS LELPEILICA SQEVRGFLGT DRVMIYRFNT
     DGSGEVVAES INNNRLPSLK GLNFPADDIP QEAREMYVNL RQRTIVDVNS GLMGLSPLDS
     AETGESLTSE EIRYRSVDTC HATYLRAMGV QSSVVVPILC DLSEQEITDH LGISQSRTQN
     LKSKTELWGL LVSHHCESNR ISETDLQLVQ LVVDQISIAI SHSNLLGQTR EQALREAKVN
     RVATLLHGQP TIQLKAALEA TVKDLQGAGG RVYFKNKNQK VKDKNISATA INPEGINFSE
     DDLPTSFELF TCGEQPSLPK WEKEIPIEEH PLWQQWAEAG FKAAGFKQIN EVSQFPIPNS
     QFSIPNSQFP ILIVTDLYKE PSFRVLVPAF QSTQIRGLLV VPLQYRQHLL GYLTIFRNEI
     ETERLWAGRF ESNVKQQLPR QSFELWRELK KGQSREWNSR EIEQVKAIGN HFSMAIQQYT
     LYKEVQNLNI NLERQVQERT SQLQQSLELA KVLGRVTDQI RSTLDLKKIL QTIVREVRTL
     LHTDRVVIYQ FIKGREGEVV VESIASLSDI TRSGRSSILG IKAPENCFPE ESACLYRQGR
     VQAINDIYQD DLAPCHRKFL ESLQIRASLI VPIGTDALLW GLLITHECSG PRVWQNSERD
     LLQQLAHQAA IAIHQAELYE ASQAAAIAEQ AKAQQLGRTL GELRHTQAQL IQTEKMSGLG
     QLVAGVAHEI NNPVNFIYGN ISHVTEYTKD LLDLVELYEQ EYPAPNDRIS EHTQAIDLDF
     LAKDLPKILD SMKMGAERIR QLVLSLRNFS RLDQADKKPV DIHEGLESTL VILQHRLKAK
     PDRPAIELFK EYGNLPLVEC YAGLLNQVFM NIISNAIDAL EMGIRDRGMR QKNLEDTGIS
     TQNSIFFTPN DTPAYIRIRT ELTDPETAVI SIQDNGQGIP QNLVSQIFNP FFTTKPVGQG
     TGLGLSISYQ IIVEKHKGVL RCISQPGEGT EFRIEIPVN
//