ID   Q8YR91_NOSS1            Unreviewed;      1804 AA.
AC   Q8YR91;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=all3557 {ECO:0000313|EMBL:BAB75256.1};
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:BAB75256.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB75256.1, 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; BAB75256.1; -; Genomic_DNA.
DR   PIR; AF2250; AF2250.
DR   RefSeq; WP_010997707.1; NZ_RSCN01000034.1.
DR   STRING; 103690.gene:10495598; -.
DR   KEGG; ana:all3557; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 573511at2; -.
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; 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   Kinase {ECO:0000313|EMBL:BAB75256.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:BAB75256.1}.
FT   DOMAIN          14..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1546..1803
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1804 AA;  202739 MW;  B0455C91274699C6 CRC64;
     MATQEYSNPI ITGYHISSQL YAGSKTRVYR AIREQDQRPV VIKLLASDYP NFHELLQFRN
     QYTISKNLNV TGIIRPLSLE TYGNGYILVM EDTGGIALRE YIKTTPFPLV EFLAIAIQIT
     NILQELHLNR VIHKDIKPAN ILIHPQTKQV QLIDFSIASL LPKETQEIRS PNVLEGTLAY
     ISPEQTGRMN RGIDYRSDFY SLGVTLYELL MGELPFSSDD PMELVHCHIA KTPIALGHQQ
     HIPLVLSDII MKLMAKNAED RYQSALGLKH DLETCLYQFK NNGKITAFEI GNRDMCDRFL
     IPEKLYGRET EVNALLQAFE RVTKGKSEMM LVAGFSGIGK TAVVNEVHKP ITRQQGYFIK
     GKFDQFNRNL PLSAFVQALR DLMGQLLSES DSQLSRWRTK ILDTVGNNGQ VLIEVIPELE
     IIIGKQHPAP ELSGTAAQNR FNLLFQKFIA IFSTPKHPLV MFLDDLQWSD TASLQLIKLL
     MEDQSYLLLL GAYRDNEVHT THPFILTVEE LKKAGKTVNT ITLASLTFCD TNHLVADTLH
     CPTERSHPLT KLIERKTKGN PFFITQFLKA LHEDQLITFN RHQGYWECDI TQINELSLTD
     NVVEFMAQQL QKFPSKTQDV LKLAACIGNS FDLNTLAIVL EKSAVDTADA LWKALQEGLI
     LPQSQVYKFY VDHDCQDANV SNSQNVEYRF LHDRVQQAAY SLIPQDQKQA THYQIGQLLL
     KQISPVAREE RIFALVNQLN YGIALITQQT ERDELAQLNL TACRKARSAT AYQAAHEYIA
     VGLSLLGKNA WQRQYKIALT LHEFAAEVAS LRGEFAQMEQ FINVVTTQAH TLIEQVNVYR
     IRIQAYISQN KFAEAIAIAQ KILQQLGVTF AEAPTPAVIQ QEIQEIRELI GDRAIADLVH
     LPIITDEEKV AIVQIASSIM TVAYLSGSPL FPLITLLLVK ISIQYGNTPA TGYIYSTYGV
     LLCNVLQDVD TATEFGQLAL QIVSKVDAKA IQPQVLLILA LYILQRKSHV QEILPLLQKG
     YAIALEVGNL EFAGHHAHNF CSHSFWCGQH LATLQEDARA YCHELGQLNQ VTTANYVRIY
     WQSTLNLLGF AAHPSILSGE ALQEPEFIPL LMAANDGYGL YIFSLYKLML CYLFGEIEIA
     KSITIEIRDH LMAAAGLFCE PVFYLYDSLI ALTQLRQNSD EVSATLQYVA ENQAKLHQWA
     QYAPMNHQHK LDLVAAERYR VLGEKTSAIE YYDRAISGAK KYHYIQEEAL SNELAATFYL
     DWGKDKVAQI YMQEAYYCYA RWGAKAKIDD LEKLYPQLLK PILQRRQLNF NPLETIAPIN
     RSTIAISTDT AGTSSTSISD ILDFTSVLKA AQAISSTIDL EELIVNLTKI ILEISGAKKI
     VLILPQDNAW YVRAITFISY ENKPEGKIQN ILLSEPIDTC QHIPGTIINY AKNTLETLVI
     DNYQIDIPGL IDQYLLKHQP KSVLCQPIIK QSNLVGILYL ENQITSGVFT LERLQVINLL
     SSQAAISLEN ACLYQKAQQA LQDLQTAQLQ IIQSEKMSAL GNLVAGVAHE MNNPLGFIAA
     TLEQAKPTIA DIAEHLRLYQ ANFPHKSAEI INHAEEIDLD YSLEDLPKMI DAMVMAGDRL
     KNISTSLRTF SRADTDYKVR FNVHEGIDSS ILILKHRLKA NEQRPAIEVI TDYGNLPQIE
     CFPGQLNQVF MNLLANAIDA LEAANKGQTF EEIKTHPKQI TITTSVHNDQ VKIIIADNGI
     GMSEQVKQKI FDHLFTTKAV GKGTGLGLAI ASQIVIEKHN GSLFVNSQLG AGTEFVITLP
     ILTR
//