ID A0A0D6KUE0_9CYAN Unreviewed; 1802 AA.
AC A0A0D6KUE0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FDUTEX481_05806 {ECO:0000313|EMBL:EKF03003.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF03003.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF03003.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
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:EKF03003.1}.
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DR EMBL; AGCR01000026; EKF03003.1; -; Genomic_DNA.
DR RefSeq; WP_045869972.1; NZ_JH930359.1.
DR STRING; 1188.FDUTEX481_05806; -.
DR PATRIC; fig|1188.3.peg.3517; -.
DR HOGENOM; CLU_000445_34_0_3; -.
DR OrthoDB; 573511at2; -.
DR Proteomes; UP000032761; 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; 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 Kinase {ECO:0000313|EMBL:EKF03003.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EKF03003.1}.
FT DOMAIN 11..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1554..1802
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1802 AA; 202451 MW; DD4FBF6B73A4C185 CRC64;
MVSTLISIPG YRISEELYNG SRTIVYRAVR ETDSVPVVIK LLKNPYPSFS ELLLFRNQYT
IGKNLNSPLI IQTYSLESLH NGYMLVMEDF GGISLKDYFS KNQRVTSREE FLVIAIALCD
ILDLLYHERI IHKDIKPSNI LINPETKQVK LIDFSIASLL PRETQTLVNP NVLEGTLAYI
SPEQTGRMNR GIDYRTDFYS LGVTFYELLT GELPFASNDA MELVHCHIAK HPPLIHEINP
DIPSVISEIV GKLMAKNAED RYQSALGLKF DLEKCLIQLK ETGEIQSFEI GQRDVCDRFI
IPDTLYGRET EVQTLLEAFE RVSQGATEIM LVAGFSGIGK TAVVNEVHKP IVRQRGYFIK
GKYDQFQQNI PFSAFVQAFR DLMGQLLSEF DAQLQIWKTK ILEVVGENGQ VLIDVIPELE
HIIGAQPPAT ELSGTAAENR FNLLLQKFVQ VFTNQEHPLV MFLDDLQWAD SASLKLLQLL
MQDTKYLLLL GAYRDNEVSS THSFIMTIDE LKKSEVLVNK IILQPLSEAK LNQLVADTLN
CELLPAQSLT TLIYQKTKGN PFFSTQFLKA LNNEQLITFD FASRNWQCDI ARIKALAITD
DVVEFMSLQL QKFPQHTQNI LKLAACIGAQ FDLQTLAIIS EQVLEATAAD LWKALQEGLI
IPNTKIYKFF VKFEHISSDY AAANPVYRFL HDRVQQAAYS LIPDEKKQVT HLKIGQLLLQ
NSAEIEREEK LFDIVGHLNQ GQVLIHQPQE RKALAKLNLK AGNKARNSTA YTAAREYFQT
GIELLEINCW QSQYELALNL YIAATEASYL NGDFDAMEQL AFLVLQQAQS IIDKVKIYEI
QIAALTASSQ ILAAIAVGRE ALAQLGVELP SQVDETQIRK ALAAVNQQLQ SREIAALIDL
PLMSEPQAQA AIQILSMLFP PVLLGIPGLM PILGATMVRL SLEFGNTPAS IPGYAIHGMV
MCAFFGEVEI GYEFGKLALS LLEKLNVPGM KCITLNLFGA FIHHHRQALL TTLIIQKESY
RAGMENGDFL YAGYSIQGYA FGRLFTGAEL NALADELHTY STALAQFKQD SARIYLDMVQ
QTVAQFRETV SQSDRLIGTF YDETVMFPKH EQDRDLTAFA FTYNYKLLLA YSFGNYHAAL
EYITQFKSYL MAVSGMFLVP LFHFYAALTH LALVSTEPEK IFAEVETHQK TLHQWAENAP
MNHLHKWHLV EAEKCRVCGD KLAAMEHYEQ AITLAKTHQF LNEEALANEL AAKFYLDWDK
EKIAQTYMME AYYCYARWGA KAKVIDLERR YPQLLLPILH KQQPTFKPTE TILSISSHTI
QSSSLSNTSL SQALDLATII KAFQSLSCEI ELEKLLSTLL QVILENAGAD KCALLMPKGD
CWVIEALSQF QQRAIILQSL PCEEIVSVSL INRVKNTLVA AVVENAVVEP TLLADPYILH
HAPKSIFCAP ILNQGKLMGI LYLENNLTLG AFTSERIEIL NLLCTQAAIS LENAKLYHQL
ENYSHNLEQK VAERTQELTT KATQLESTLN QLYSTQAQLI QAEKMSSLGQ LVAGIAHEIN
NPINFIYGNL SAANEYVTSL IELNHLYQSI YPQTLPEIAQ KIADIDLEFI LNDLPNLLSS
MKVGAERIRQ IVLSLRNFSR LDESEIKEVD IHSGLESTLL ILQHRLQSNS KRPEIILSKQ
YGVLPLVNCY ASALNQVFMN IINNAIDALE TSDNNRQPTI MIKTELTETK NVIIRIADNG
IGMNQSVQNQ IFNPFFTTKP VGSGTGLGLS TSYSIVVEKH CGQLSCISAP GEGTEFIIKI
PV
//
