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Database: UniProt
Entry: K9TGI8_9CYAN
LinkDB: K9TGI8_9CYAN
Original site: K9TGI8_9CYAN 
ID   K9TGI8_9CYAN            Unreviewed;      1818 AA.
AC   K9TGI8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Oscil6304_2349 {ECO:0000313|EMBL:AFY81977.1};
OS   Oscillatoria acuminata PCC 6304.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY81977.1, ECO:0000313|Proteomes:UP000010367};
RN   [1] {ECO:0000313|EMBL:AFY81977.1, ECO:0000313|Proteomes:UP000010367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY81977.1,
RC   ECO:0000313|Proteomes:UP000010367};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003607; AFY81977.1; -; Genomic_DNA.
DR   RefSeq; WP_015148619.1; NC_019693.1.
DR   STRING; 56110.Oscil6304_2349; -.
DR   KEGG; oac:Oscil6304_2349; -.
DR   PATRIC; fig|56110.3.peg.2789; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_34_1_3; -.
DR   InParanoid; K9TGI8; -.
DR   OrthoDB; 573511at2; -.
DR   Proteomes; UP000010367; 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};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010367}.
FT   DOMAIN          18..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1569..1818
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1530..1560
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1818 AA;  203678 MW;  2A04EC8A9492CFCF CRC64;
     MKNPEMMTGQ SHPQLPDYTL TELIYPGTRT HVYRGVHQQS QQPVVIKVMK RDYPTFGELV
     QFRNQFVITK NLQIPGIVRT LALEVFGNGY AIVMEDSGSI SMEQYLENQS LNLLKILDIA
     IQLTTILHDL HHHRIIHKDI KPANVLIHPN SRQITLIDFS IASLLPKETQ EIQSPQGLEG
     TLAYLAPEQT GRMNRGIDYR ADFYALGVML YELLTGQLPF RSDDPLEVIH SHIAKTPTPV
     HEVNPEIPAM LEAIVAKLMA KNAEDRYQSA LGLQHDLREC LNQWQTRGEI SEFVLGQRDL
     SDRFNIPEKL YGRETEVQAL LKAFERVSQG ASELMLVAGF SGIGKTAVVN EVHKPITEQK
     GYFIKGKFDQ FNRNIPLSAF VQALRDLIGQ LLCESDVELA QWQAQILEAV GENGQVLIEV
     IPELEQVMGQ QPPTPELSGS AVQNRFNLLF QKFIQVFTTA AHPLVIFLDD LQWADAASLQ
     LLKVLMDDNG YLLVLGAYRD NEVSPAHPLM LTIAELKKAN FTVNTITLAP LSLEHTNHLI
     ADTLKCSRER AQSLTQLVDR KTQGNPFFTT QFLKALHEDG YITFERNQGY WQCDIAQVNA
     LALTDDVVEF MALQLQKLPG ETQQILKLAA CIGNQFDLAT LAIVAEQSLT EAATALWNSL
     QEGLIVPITQ IYKFFHAEEI ESADVHNSIT PVYRFLHDRI QQAAYSLIPE DQKQWTHYHI
     GQLLLKQTSP TTREEQVFEL VNQLNHGISL ITHPSEQFEL AQLNLIAAQK ARAAAAYEAA
     QNYVTLGLAL LGEEAWEDHY EIILVLYELA AEIAFLIGDF PQMEAWINTV IAQAHNLLDK
     INVYQIQIQS IVSQAKFAEA LIIAQEILQE LGITFMATPT FADIQKEIQE ITELMGDREI
     IDLLHLPENV DQLKLAIIQM TTGVAPAAYL SGSPLFPFLI SCAVKLSIQS GNTADSALAY
     SLYSIVTCNF LQDVDTATAF SQLALQLVAK LDAKAVKPEI YSAVGLYILH RKSPVTATLP
     LFFEGYTAAL EVGNLEYVAF NANEFCTYSF WCGQPLTTLE QESRDYCQAL VNLNQLGVAN
     YCCLCWQSTL NLLGRSDDPT LIAGEAIQET ELLPFMLSAH DLAGLYFFYL YKLVLCYLFG
     KIDLANHDAL EIRNYLMAGA GTLGEAVFYF YDSLIALAQL PSVTEEQAST LEERVERNQT
     QLQFWAHHAP MNHQHKVDLV SAERCRVLGQ SYEAGNYYDR AIARAKENSY IQEEALANEL
     AAKFYLDWGK EKVAAGYMQE AYYCYARWGA KAKVEDLEKR YPQLLQPILQ AANQPLTVLE
     TLTSIATSSV YSIHATSSKS ESSSSINQTL DFAALLQISQ TFASTIALDE LLQTLTQTML
     ENSGADRCAL MLCEDKQWQV RVLANLKQVT LQSAPLNDNP NVPVKLIQYV KNTVTTVVLD
     ALKTDLPVIG DYLHRHQPKS VLCLPILNQG NLLAILYLEN RSASGVFTGD RIVILNFLCT
     QAAISLENAS LYQKVSNYSH TLEAEVVRQT QVLHQKNQEL EQILKNLQQT QAQLIQNEKM
     SSLGQLVAGI AHEINNPINF IKGNIAPLEN YWKDLKNLVN LYREDGCQPS ESLQMKQEEV
     DLEFLFRDVE KILKSMTTGS ERIQQIVLSL RNFSRLDESS TKAVDLHSGI DSTLLILQHR
     LQQIGDSPEI QVVCDYGDLP RITCYPSQLN QVFLNIINNA IDAIRENSKC SDHPQIRIRT
     EPLAQKGIRI AIANTDSRIP PEIQDRIFDP FFTTKPVGSG TGLGLFVSYS IIQKHGGTLR
     VRSPSSGGAE FEIILPCG
//
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