ID   Q9L708_NOSS1            Unreviewed;      1777 AA.
AC   Q9L708;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=hstK {ECO:0000313|EMBL:AAF44653.1};
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:AAF44653.1};
RN   [1] {ECO:0000313|EMBL:AAF44653.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11736654; DOI=10.1042/0264-6021:3600639;
RA   Phalip V., Li J.H., Zhang C.C.;
RT   "HstK, a cyanobacterial protein with both a serine/threonine kinase domain
RT   and a histidine kinase domain: implication for the mechanism of signal
RT   transduction.";
RL   Biochem. J. 360:639-644(2001).
RN   [2] {ECO:0000313|EMBL:BAB73957.1, ECO:0000313|Proteomes:UP000002483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 {ECO:0000313|EMBL:BAB73957.1}, and PCC 7120 / SAG
RC   25.82 / UTEX 2576 {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; AF230361; AAF44653.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB73957.1; -; Genomic_DNA.
DR   PIR; AC2088; AC2088.
DR   RefSeq; WP_010996415.1; NZ_RSCN01000004.1.
DR   STRING; 103690.gene:10494287; -.
DR   KEGG; ana:alr2258; -.
DR   eggNOG; COG0515; 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; 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:AAF44653.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:AAF44653.1}.
FT   DOMAIN          7..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1518..1776
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1468..1499
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1777 AA;  200912 MW;  81D5684741F76A24 CRC64;
     MITLPNYQII ELIGEGVKTN VYHAISIPDS KLVVIKILKT EYPELKDIAA LKHEYELIKN
     LDIPGVVKAH GFEKYNNCFA LVLEEFDGTS LHKVIQEKKI GLLDFCKIGI QITQALGELH
     RKYIIHKDIK PQNIIVNLET HQVKIIDFSI SSLLFQEKAK LNNPNLLEGT IAYMSPEQTG
     RMNRSIDYRT DFYSLGVTFY EMLTGQLPFI VTDPMELVHC HIAKQPISIN QLIPEIPEVV
     SEIIMKLLSK TAEERYQSAL GIKADLEKCL NQLVAVDSIT TFPIGQHDQS SQLQIPEKLY
     GREAEIDILM AAFENVNQGH KELILVAGYS GIGKSALVNE IHKPVIKNRG YFIAGKFEQF
     QRNIPYASLI QAFQELMQQL LTESGQQLAN WRERILAALV PNAQIIIDVI PELELIIGKQ
     PEVPQLGSAE AQNRFNLVMQ KFINVFAQKE HPLVVFLDDL QWADLASLKL IQLLAINSDI
     QYLFLIGAYR DNEVDSSHHL MLILQEIEKN RTPINIIYCQ NLKITDVCQL VGDTLKSGLE
     DSKELAKLIF HKTGGNPFFI NQLLKFIHQE NLLVFNFITG QWQWYIQYIQ MLDITDNVVD
     LMIGKIQKLK DNTQNIIKIA ACIGNRFNLN TLSCINEKSH NATALDIWEA LQAGLIIPLS
     DNYKLPQLLD DVDIFVIDYK FLHDRVQQAA YALIPDEHKK EIHLNIGRLL LKNIDKSLLE
     EKIFDIANQL NMGAGLITAP EERYKLAALN LMAGRKAKDS TAYESAVSFL KQGLNLLDID
     CWQKHYELTL DLHVETVESA YLNTNFEEAE PLFATVIANS KNILDAVKVY EKKIQFYVGQ
     NRMREALDLD LQVLGMLGVS LSQTPPAELK IEELINLPEM MDPSKLAAMR ILMTAMPPAY
     LADPALLPLI AFTMIDLCLQ YGNSSFAAYA YGFYGLILCG PLNNIESGYR FGKLSLQILN
     QFNAKEIKSK VYALFNIFVR HWKEHIQTTI EPLQEGVQSG LDTGDIEYVG YNGLLVCWHP
     FWSGENLETV EQRLDKYINL AQRIQQEHFT VCLLILKQLL TELKQGLKNE VYLDGDDFNN
     SIMQRMAGNI TAIFYAYLAK SILSYFFKDY SQAVKNAELA QQYEVAVGGT FYLIEYKFYY
     SLALLALCLN LTSDADITSA LEKVSENQQQ LKEWADHAPI NNQHKYELVE AEKARVLGQV
     LIAMEYYECA IQGAHKFGYI HEEALAYECA AEFYFSLGRN EFACLYITKA HYGYRHWGAS
     AKVRNLESKY PELTAKISSQ YPADFTNTNI TTSTASEKSS GLDLISVIKA SQTLSEVILL
     DNLLEKLMTI VIENAGAQTG ILLLEKAGNL LIEAKASVDK DDVTVGQSIP FEDSQQLPIS
     VINFVRRTRK DVVLSDASNE GSFILDPYII KQDIKSIICT SILNQGKLIG ILYLENNLIV
     GAFTADRIQI LKLLSTQAAI SLENARLYAN LEEKIEERTR ELNENNLRLR QTLHELKLTQ
     TQLIQTEKMS SLGQMVAGIA HEINNPVSFI HGNLSHIDNY ANDLLTLIDI YRSIYPEATP
     EIEEFLENID VDFIKEDMPK TLSSMKIGTQ RIREIVLTLR NFSRLDEADM KPVDIHEGIE
     STLLILQSRL QAKPGKPAIE IIKNYAELPK VECYTGQLNQ VFMNILNNAI DSLEKLNREH
     NLEEIKTDAS AIAIRTEVVN PDLVAISIKD NGLGMSDSVR QRIFDPFFTT KPIGQGTGLG
     LSISYQIVVD KHRGSIECIS TPGQGAEFII QIPCRQK
//