ID A0A218QSL8_9CYAN Unreviewed; 1738 AA.
AC A0A218QSL8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES4075_59010 {ECO:0000313|EMBL:GAX44882.1};
OS Tolypothrix sp. NIES-4075.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX44882.1, ECO:0000313|Proteomes:UP000198313};
RN [1] {ECO:0000313|EMBL:GAX44882.1, ECO:0000313|Proteomes:UP000198313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX44882.1,
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:GAX44882.1}.
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DR EMBL; BDUC01000009; GAX44882.1; -; Genomic_DNA.
DR OrthoDB; 573511at2; -.
DR Proteomes; UP000198313; Unassembled WGS sequence.
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; PF00512; HisKA; 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:GAX44882.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000198313};
KW Transferase {ECO:0000313|EMBL:GAX44882.1}.
FT DOMAIN 8..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1530..1738
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1464..1523
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1738 AA; 195956 MW; 9B6A3B27EF2C0358 CRC64;
MMSALPGYTL GTILHNGDRT LVYRSIQECD QKTVVIKTLK AEFPTVEETA RLKQEYQILM
DLPLEGVIKP YKLEQYQKRL ALILEDFGSD LKTFVADKIA LTDWLEIAIQ IASILGEIHQ
HQIIHKDIKP KNILINSHRQ VKIIDFSIAS RLSKENPLLS PPSLLEGSLH YLSPEQTGRM
NRAIDYRSDL YALGVTFYEL LTQRLPFQSD DPLELIHAHI AKQPIPPHQV RQDIPVVISN
IIMKLLAKNA EDRYQSAFGV KKDLETALEQ LTTTGEIKEF AIAQHDTSFH LLIPQKLYGR
ETEVATLMQA FARIAKVEKI ELLLVSGYSG IGKSSLVNEI YKLILQQRGY FIAGKFDQFQ
RDIPYASLIQ AFRMLMQQLL AESAASLEVW KTKLQQALLT NAQLIIEVIP EVELLIGSQS
PVPTLGATET QARFNRVFQA FINVFAQKEH PLVLFLDDLQ WADSASLKFI QALINDANIG
YLLLLGAYRD NEVSAAHPLI QTIAQLQETG ARINQIVLKP LSLESVKQLV ADTLQETETS
TQLATLLYNK TDGNPFFLTQ LLQSLAQINL IKFDFATARW TWDLTQIQTV GVTDNVIELM
VNKIEKLPKK TQFLLKFAAC IGYRFDLETL AVISQKSVSE TAKEIWSAMQ AGLILPLNNA
YKIPLFVGEE TAAIALDEHT INYQFLHDRV QQAAEALIPE AERKATHLKI GQRLLQSQSP
SEQKENIFEL VNHLNYGKDL ISDEQQRTQL AALNLIAGLK ASSAIAYEPS ARYFDLGLEL
LANDCWEQQY DLTLSLYCRL IDVECINANF TRSQSLINSA LPHTKTLLDR IRIYKLQIKL
EIAQGNSAAS IETALKALLL LDVRIPTHDA EIESYIAQLQ QKLVFRPNDV AALANLPVMS
DANKQAAIEI LNTMPGPVYI ARPQLFIPMM LTMTQLSVEY GNWIPSSFAY CLFGFMSAAI
FDNIDIGYEF GQLSLKVLEQ FNDKTLYPHV LKVYGSHVHF IKNSLRSTLK FLQVSVERAM
EVGNLEFVGY GTSEYVMHYF FSGENLEIIN QKALPYVELV DRAKQELGIY YIRIARQVVL
NFIGLADDLL VLTGESFNEA TMLPSVSAGN WQTLLCCFYL FKLMLAYRFG DYEQASIHAK
STAANLQAVV GMMMMYEYIF YDSLTLLQCD DDREVLPQVQ ANQAILKQKA DYAPMNFQHK
YELVEAEIAR VTGQTLLAMN AYDASIQSAK NHEFTQDEAL ANELAAKFYL GINKPKIAAA
YLNDAYLGYI SWGSQPLAEN LLTRYPDLLP HIRGSTSTTL STTAAWLDLS TAVKASQAIA
SELRIKNLLN RLIAIVIENA AAQRGFLIAE KAGEFTIVAA GTIDQNQIIS PSSQTELPNS
ILNYVVRTRE SIVLNHATKE GIFINDPYIR EYQPKSVLCT PIIHQGQLKN LLYLENYITT
GAFTVERLEI LKLLSAQIAV SLENSQLYEN LAQTNAELAA ANSQLEQYTQ TLEATVAERT
LELQQKNTRL EQTTAQLTLI NKELESFSSS VSHDLRSPLR RIDYFSQMLA ESLNDSLTAT
RQNYLNRIQN STQHMRQLID DLLRLSQISR SQLHRTQVNL STIVQAIAED LEKDQPRQVK
FQITPDLTTS ADANLLRAAL ENLLGNAWKY TRNREYTQIY FGKLDNNVFF IRDNGVGFDM
NNSDNLFQPF QRLHSAKEFE GNGIGLATVA RIIHRHGGRI WAEGKVGEGA TFYFTLEG
//
