ID A0A218QTT2_9CYAN Unreviewed; 2011 AA.
AC A0A218QTT2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES4075_62070 {ECO:0000313|EMBL:GAX45186.1};
OS Tolypothrix sp. NIES-4075.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX45186.1, ECO:0000313|Proteomes:UP000198313};
RN [1] {ECO:0000313|EMBL:GAX45186.1, ECO:0000313|Proteomes:UP000198313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX45186.1,
RC ECO:0000313|Proteomes:UP000198313};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX45186.1}.
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DR EMBL; BDUC01000010; GAX45186.1; -; Genomic_DNA.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000198313; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:GAX45186.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198313};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1567..1783
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1807..1923
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1508..1567
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1856
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2011 AA; 227525 MW; 0980DC080BF9A9D5 CRC64;
MSITIAGYNL IEVICEGTTT CVYRATREPE QTSVIIKTIK TEYPTIEQLT RLRHEYQILQ
SLEIEGIVKP LAWMSDRNGL ALILSDFGGE PLKNFITAQN LDLSNFLQIG IQLSSTLAQI
HQNNIIHKDI KPQNILINAK TGQVEIIDFS ISSHLSRENQ TISNLNLLEG TLAYMSPEQT
GRMNRSIDYR TDFYSLGVTF YEMLTGQLPF QATDFLELVH CHIAKTPATP KEVNSEIPQA
VSDIVMKLLA KTAEQRYQSA LGLKADLEEC LNKVQATGTI EDFIVGQLDS YSQFIIPQKL
YGREKEVASL INAFDRVSLG ATEIILVSGY SGIGKSSLVN EIHKPIVRQR GYFISGKFDQ
FKRNIPYASI IQAFQELIRQ LLTESAEKVA VWKAKILNAV SSNGQVIIDV IPEVERIIGS
QPAVPQLAAT ESQNRFNRVF QQFIHVFCQP EHPLVLFLDD LQWTDSASLK LIQLLACDLN
SQYLLLIGVY RDNEVSATHP LMLTLEEIQK TNAVVNNIVL QPLHITHVNQ LVSDTLRTDQ
QKSQPLAKLL FNKTQGNPFF LTQLLKSLHQ ENLLSFNFSH GCWQWNIELL KDIDITDNVV
ELMVNQIQKL SPTTQNVLKL AACIGDKFSL DILSIVNQTY LSQTAVDLWE SLQAGLVLPL
DESYKIPLVG EWGDKETRRQ GDKETRESFL LSYPFPLLKM PNAQFPIAYK FLHDRVQQAA
YSLIADSQKK ETHLKIGRLL LQKTTLEERK ENIFALVNQL NYGTDLLTLK SEKYELAELN
LIAGQKAKAA TAYESAIRYL KVGLNLLTAN SWEEQYEITL ALYELAVETA YLNGDFQQME
KWATIVLQQA KTFIDKMKVY EVKIQACMAQ VKQLEAVKIG LEALELLGVR FPLPTDLDIE
QTLSQTAINL TGKSIEDLIN LPLMTEVDKL AAIRMLTSMG SPTYQAAPAL FPLIVCEHVN
LSIKYGNAPF SAYGYVCYGV ILNGVIQDID SAYKFGKLAL NLLERYNVLE IKTSVFFVAA
ACTIHGKVHV RDTLPLLQDG YESGLENGHF EYGGYAAMQK CQYSYFIGQE LTSLEREMAT
ISNSLTQLKQ ENALSWNQIF QQSVLNLLEF CENPCCLLGE VYNQEKSLPL LRKANDRTGL
HYFYLNKLIL CYLFGEYQQA WENAAYGSEY LDGVKAFLVV QVFHFYDSLA QLAIYSSASH
SQQEHLLNRV INNQEKMQKW AEHAPMNFQH KYELVEAEKA RVLSQYWQAM EFYDRAIAQA
KNQGYIQEEA LCNELAAKFY FESGREKVAQ TYLTDAYYGY IRWGATAKVK DLEARYPHIF
SQISQGKTKV EISQTIRSTT INSPGFLDLA AVMKASLALS GEMVLDKLLA KLMQIVLANA
GAETGFLILE KAGQLFIEAS GSVGHEIMVQ QSTSIESSQQ LPISLINYVR STQENIVLND
ASRQGVFTTD SYILNKKPKS ILCTPIVNQG KLIGILYLEN NLTIGAFTPE RLEVLQLLSS
QAAISIENAR LYNDLEEYNQ TLSAKVEERT LELQEKNLQL QQEIKERQRA EEAAKQANRA
KSEFLANMSH EFRTPLNGIL GYTQIFQKDK NLTSQQKNGI NIIHQCGEHL LTLINDILDL
SKIEARRMEL EAKEFVFPEF IESIADICRI RAQQKGISLI YKTFSPLPKV IRADEKRLRQ
VLINLLSNAV KFTEKGCITF KVGYQKEKLR FQVEDTGIGI AQEQLKEIFL PFQQVGEHSR
KIEGTGLGLA ISHQLVQLMG GELMVKSTLG KGSVFWLELD LPEVLQEINV NSVDRRHIIG
YLGSKRKVLV VDDKWANRSV LLNLLEPLGF EVAEATDGLD ALNKAHEFKP DVIFMDLVMT
VMDGFEATRR LRMLPDLKEV VVIAASASVF DFDQKQSREV GCDDFIPKPI REGELLEKLK
IHLGLEWVYE EQKSREELSS PLRTQDSFVA PPAEELAVLL DLAMRGDLRG ITKRAIKLEE
LDERWIPFAT HLRQLAKGFK GKQILEFLKQ Y
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