ID A0ZKG0_NODSP Unreviewed; 1287 AA.
AC A0ZKG0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NSP_45300 {ECO:0000313|EMBL:AHJ30826.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ30826.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ30826.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ30826.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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; CP007203; AHJ30826.1; -; Genomic_DNA.
DR RefSeq; WP_006198239.1; NZ_CP007203.1.
DR STRING; 313624.NSP_45300; -.
DR PATRIC; fig|313624.11.peg.4539; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_257991_0_0_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
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; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..353
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 528..580
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 898..1135
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1165..1283
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 293..320
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 871..898
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1214
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1287 AA; 143470 MW; 1725DF235A25ECCD CRC64;
MFKINPLQLE YLHRLRVVQA ASAIAILVGV LVLLGWFFDL ELLKRSGNNL VTMKPNAALG
FLLSGLSLWL LQMAQGKKDN SSIAYLRGSR ICAAIVTLIG LLTLSQYLFG WNLGIDELLF
TDKPDAIFTS HPGRMGFNTA LNFILVGIAL EILAHPKNNR SCWYVQILAL IAALISLQVV
ISYAYKVQIF SRIASFTTSM VLHTGLTFIV LCVGILWARP DKGLMQVVMS DTYGGLIARR
LLLAAIAIPL VLGWLILQGQ LAGKYGSAFA LLLFAIILII IFTIFIWQSS TVITRLCRQH
DEAQKKLRAY EEKLRSFVDA NVIGIKFGDV YGGIHEANDA FLQMIGYTRE DLLTGKLNWR
NITPPEHVYS DKQGIAEAQG NPNGACTPYE KEYIHKDGRR IPVLVGYVLV GENREESVVF
ILDLSERKQA KQQIVQLNKD LQRRIAELQT LFQVIPIGIG IAEDAECKTI RANPCLAQQL
GVSSDENVSL SAPSAERPTS FKVYREGREL LPEELPMQYS AAHGVEMLNC ELDIVHENGK
VVKLLEHVAP LFDEEGDSRG SVGAFLDITE RKQVEETIQN QQKWLEDVLN MMPMPLLFIE
PGTGRVIFAN RAVDDLAGGE FPKGIPVEEY HTAYYCTDMA GNRIPNDQIP GARIARGERL
DGLEMDWHTK ESVRSIRIFS DTLPAMHGHP ATCVSAFQDI TNLKEIEKAR TLNYRRLQLL
FNTASDLLSS QQPLALIHSF YQKLAEQIGL DVYFNYLAED HSQVMHLVSF TGVSEEIAKE
YECLKFGQSV CGIVAQERHP IYIENVQQST DPKTELIRSL GITAYYGYPL IASARLLGTL
CFGSRSCSRF TENQRGMMQA VSDQIAIAME RSSLIASLQQ QTEQLREANR MKDEFLAILS
HELRSPLNAI LGWAQLLRSR KLSDIQIAKA METIERNARM QTQLVEDLLD ISRMIRGKLH
LHVCTCNLVP LIESAVETVH LAAQAKEIDL RISLIPSPEM PQDHSRFLVS GDIERLQQII
WNLLSNAIKF TPTGGRIEIR LCQSVEDDEK LARTITSYAQ IQVIDTGIGI KPEFLPYVFD
RFRQADSSST RSYGGLGLGL AIVRHLVELH GGIISVDSQG ENEGATFTVK LPLLLESQAV
IPDSVNQNNA DFAYPSPVPS LLGVRVLVVD DEMDTRDFIS TVLEECQAEV KAVKSVSEAL
QVIIDWKPDV LVSDIAMPEE DGYSLIRKVR SQPQEQGGKI PAAALTAYAR AEDRTRAIQE
GYQLHLPKPI EPAELATVVA SLVIRNS
//
