ID A0A218QRU3_9CYAN Unreviewed; 1778 AA.
AC A0A218QRU3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES4075_56870 {ECO:0000313|EMBL:GAX44668.1};
OS Tolypothrix sp. NIES-4075.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX44668.1, ECO:0000313|Proteomes:UP000198313};
RN [1] {ECO:0000313|EMBL:GAX44668.1, ECO:0000313|Proteomes:UP000198313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX44668.1,
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 + 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:GAX44668.1}.
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DR EMBL; BDUC01000008; GAX44668.1; -; Genomic_DNA.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000198313; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAX44668.1};
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 130..184
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 364..581
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 668..783
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 799..845
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 916..979
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 991..1044
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1045..1100
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1118..1170
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1369..1633
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1657..1775
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 716
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1706
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1778 AA; 199139 MW; 88C153F389338EC3 CRC64;
MQDKESDYQL ESDRSTSPDY QQEHIFPGNG EMSLLMRTLD WSVTPIGSVE HWTQSLRTSL
SICLSSRFPI LIWWGKELVM LYNDAYRPIL GTTKHPQALG QSGSECWSEI WDIIGPMLEG
VMITGNATWS DDQLLLIDRN GYLEECYFTF SYSPIRDETG GIGGVFTAVT ETTERVLSER
RLRTLRELAA KTSQAKTVEE ACELSMETLA DNVADIPFAL IYLLDEAGKQ AKLIKAGGLA
PQEIACQETL DLLSDDTHSL PLVKVVRTGE PERVNNWGPS SYADLADSAL ILPITQANHD
LPAGLLVVGI NPRRALDEEY SGFFQLIAGN IATAIANARA YETERKRAEA LFELDRAKTT
FFSNISHEFR TPLTLIIAPL EEMLRRLQQF APQDQEQLQL IHRNSQRLLK LVNSLLDFSR
IEAGRVQAVY EPIDLAAFTA ELASLFRSVI EAADMRLIVQ CLPLRSSVYV DRQMWEKIVL
NLLSNAFKFT FQGEITLTLR ECQNYVELEI SDTGTGIPES EIPHLFERFH RVKGAKGRSF
EGSGIGLSLV QELVKLHGGT ITVSSIVDQG TSFVVSIPTG YAHLPSVNIG AINTLASTAI
GATSYVEEAL RWLPAEGTGD SLLGGKGERE KGKGKELLPI TDYPLPITHY RLPITHYPIP
NPQSPISRIL LADDNADMRD YVKRLLQQNY QVEAVGDGLA AASAIRQQPF DLVLTDIMMP
GLDGFELLRQ LRQDPLTKEI PIILLSARAG EESRIEGLEF GADDYLVKPF SARELLARVE
ATIKLSKMRQ SMKQVLQDAN EHLTNVLENM TDAFVAFDRE WRITYVNQQT ARINNMQPEE
MIGKTQWEMW SWSIGTIIEQ KYRQAVAEQT PVHFEVLYEP LMMWLEIHAY PSKEGIGIYF
RDITTRKAAE TSLQNALQRL NFHVENSPLA VIEWDHEFRV SRWSSEAERI FGWQASEVIG
KNFQDWQFVF TEDLEVVTDA ATRLTGRVNI GNSCYNFSYT KDNSIVYCEW YSSTLFDESG
KLISVLSLVL DVTERKVMEA ALRESEERFR EMADASPTLI WMSDPSKLCN YFNKTWLEFT
GRTIEQEMGN GWTEGVHPED LQYCIDIYIN AFDAREKFSM EYRLKRYDGE YRWILDKGVP
RFTSSGNFLG YIGSCIDISD RKIAEAEREE MLVRSQQYAS QLRGLTEAAL TINSALSIEE
VLQVITERSR FIIGAHQSVT SMTIDNNWAQ SINAVSLSDK YAPRRDYKQP TDSSGIYAYI
CQINRPIRMT QSELEQHPQW HFDTETANPP MRGYLAAPLT GRDGSNIGLI QLSDKYDAGE
FTAEDEAILV QLAQMASVAI ENTRLYEAEQ LARTQAESAN RIKDEFLAVL SHELRTPLNP
ILGWSKLLRT RKFDETKTAE ALATIERNAK LQAQLIEDLL DVSRILRGKL TLNVDKVSPG
SIILAALETV RLAAEAKSIS IVTIFDLNVG QIAGDAGRLQ QVIWNLLSNA VKFTPNGGRV
EVRLSVEWGS GEWGKRGVGE AWCGGVGKSP MPNSQFPILN SQLPITNSQF SITNSYAKIT
VSDTGKGISP EFLPYVFDYF RQADSATTRK FGGLGLGLAI VRQLVELHGG TVFVESLGEG
QGATFTVKLP LFSTTDSLPI EFTKEAELNS FNLEGIKILI VDDDADSRDF ITFVLQQEKA
EVIAVDSALS ALQILAKSKP DVLLSDIGMP EMDGYMLIKQ VRKWLPEQGG EIPAIALTAY
AGEYDRKLAI SAGFSYHVPK PADPAQLIAA VTKLTNKS
//
