ID   Q8YYG4_NOSS1            Unreviewed;      1850 AA.
AC   Q8YYG4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=all0886 {ECO:0000313|EMBL:BAB72843.1};
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB72843.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB72843.1, ECO:0000313|Proteomes:UP000002483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC   {ECO:0000313|Proteomes:UP000002483};
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; BA000019; BAB72843.1; -; Genomic_DNA.
DR   PIR; AC1917; AC1917.
DR   RefSeq; WP_010995060.1; NZ_RSCN01000006.1.
DR   STRING; 103690.gene:10492899; -.
DR   DNASU; 1104480; -.
DR   KEGG; ana:all0886; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 517727at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAB72843.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:BAB72843.1}.
FT   DOMAIN          7..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1571..1828
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1521..1562
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1850 AA;  208948 MW;  0724B705EA682E3F CRC64;
     MLRLVGYQNL TQIYAGTRTL VYRGIREEDQ KPIVIKMLRY EYPSFSELVQ FRNQYTITKN
     LHISGIIKTY SLENYENSYA LVMEDFGGVS LKDWSIQNSE ISLDEFFHIA IQIVTILDGL
     YRSRVIHKDI KPSNILINPI TKEIRLIDFG IASLLPRETQ TLTSPNVLEG TLAYLSPEQT
     GRMNRGIDYR SDFYSLGVTF FELLTGQLPF YCDDPMKLLH CHIAKRPPQV HDINSTIPLA
     VSNIAFKLMA KNAEDRYQSA LGLKHDLETC WKQWQTQGEI SVFELGSRDI CDRFIIPEKL
     YGRQAEVQQL LAAFERVSQG NREMILVAGF SGIGKTAIVN EIHKPIVKQS GYFIKGKYDQ
     FQRNIPLSAI VQSFQDLMGQ LLSEANTQIQ DWKTQILAAL GEQGQVIIDV IPELQSIIGQ
     QRQVTELEPS AAQNRFSTLF LKFIQVFTTK EHPLVIFLDD LQWADSASLK LIQLLMSQID
     NHYLLLIGAY RDNEVSSGHP LILTLQDIQK HAENIETITL KPLNTLDLNY LVADTLKCTT
     EVALPLTQLV YQKTQGNPFF SNQFLKYLYN ENLISFNFEK GFWECNIAQV KTLSLTDDVV
     DFMSLQLQKL PEVTQNVLKL AACINNHFNL SVLANIYEKS LPETAAALWT ALREGLIIPT
     NKVYRFFQED LSLDDSQKLN NNIEPITVEY KFLHDRVQQA AYTLIPENDK NFTHLKIGQL
     MLVNSTPEIR EEKIFEIVNQ FNIGVDLITA APARHELAQL NLQAGTKAKS ATAYGAAVEY
     INSGIELLTA SCWEDQYELT LSLYLEAVEV AYLSTEFHRM EILAETVLEN AKALLDKVKI
     YSIKIQACIA QNQLLLGIET ALPVLQMLGV NLPPKPTQTD IVKSLQAANS VLMGNKTSDL
     INLPKMDNPE KLAALSILSS MFGAAYNGYP AMFPPLICEE IILSVKYGNA PVSAFAYASY
     GAILLTFMGD IDAGYEFGNL ALNLVSKLDA KEIKAKTFCV VNCLIKHWKK PLKSTFPLFI
     EGYHSGWETG DLEWSAWCAF SYTLYLYLSG TELYSLEQEM SSYAQAIAQF KQKTSLNYLN
     IYYQSVYCLL GDTENQLQIK GHIYDEEVML PIHQQASDRP AIYHLYINKL ILCYLFCDYE
     QAIKHAEIAE QYLDGVLGIY VVVLLPFYDS LARLALYPHT TVDIQQEILH KVSENQAKIK
     QWADYAPMNH QHKFYLVAAE QNRVLGKYLE AMNYYDLAIA EAKENKYLQE EALASELAAK
     FYWESGKEKI AQVYFTDAYY AYTRWGAIAK VKDLEQRYPQ MFALLSRRSN LIFNPNDTIV
     KNDSTSSHIH QTQQNTHYYS TTISNVLDLS SVIKASQTLA SEIKLEKLLS TLMELVIENA
     GAKKCVLVLL KNERLLIEAI AKINQVPIST ILVSIPIAES DEIPISLINY VSHTSQTLVI
     DDATTEDLFI SDPYIQQKEP KSLLCTPIIK QGKLMGILYL ENHLTTGAFT SDRLQVINLL
     MAQAAISLEN AQLYGQLAEY SQNLELKVEQ RTQELKEKAN QLESALQKLS STQSQLVQAE
     KMSSLGQLVA GIAHEINNPV SFIYGNLTYT SEYVNSLLEL INLYQKLYSQ PLPEIQQKIS
     DMELDFITED LPKMLKSMRF GAERIEEIVS SLRMFARLDE AGIKRVDIHS GIDSTLLILQ
     HRLKFKQNRQ SLPIAVKQNY GNIPQIYCYA SELNQVFISI LSNAIDALQE DVSNQPGREK
     QPTITISTEV KNAESILIRI ADNGPGMSNA VLGKIFDPFF TTKPVGSGTG LGLSISYAIV
     VEKHGGQLLC SSSPGMGTEF TIEIPIQTFD TAISRETTNT NAKLRKCESA
//