ID W6FTE6_NODSP Unreviewed; 949 AA.
AC W6FTE6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NSP_39660 {ECO:0000313|EMBL:AHJ30267.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ30267.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ30267.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ30267.1};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007203; AHJ30267.1; -; Genomic_DNA.
DR AlphaFoldDB; W6FTE6; -.
DR STRING; 313624.NSP_39660; -.
DR PATRIC; fig|313624.11.peg.3980; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 1..99
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 406..640
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..785
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 822..939
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 273..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..369
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 40
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 872
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 949 AA; 106532 MW; 8213E6532A340674 CRC64;
MQFLEEARDY LNTLEAVLLE IDNTNRIDLD RINAALRAAH SIKGGAGMMG FRTLSDLAHR
LEDSFKVLKT RKNSRELDTH LPSLLLSGVD WLRQILESLS QGHEIEEQYL SSFCYPVFDE
LRDRLGEPTP EDAFTMLSPE DGQDIVPMLF ETEVEGCLQR LESILADSAH PGLQEEVVIM
AAELGGLGEM LQLTAFTSLC ESIEHHIGNA NSDRLREIAQ LALQTWRRSQ ALILTNQRDS
LPTQLDLDTP FNYITSPPQT TTSARAEFLE DTEPTDDFTS VDIPAENPVI SPENSPTDEQ
INLGKDWENS ENTVRVPSKK LEEINDLFGE LTVQRNGLNS QIEKLRNLVR NLNQRVQTLD
RENYELRTAY AKITKTAGGK FLESNNVENL PESDTLEGDG HQKLNVRSQE VMETIVQVQE
ITSDIQLSIE DTDQITRKLN KTSKQLQTKL THIRLRPFSD LIERFPRALR DLNIEYGKNV
HLQVEGKKIL IERSILEALN EPIMHLLRNA FDHGIEDPVT RRQLGKPEQG LIEITATHSS
NRTIITMRDD GRGISLEKIR SRAVTMGLDA ALVANASEEE LLSLIFEPGF TTSDQVTALS
GRGVGMDVVR NNLKSVRGDI TVNTELGVGT TFTLSVPFTL SVARVLLVES NKMLLAFPTE
VVSEIFLLPN EQVFSVADNE VINWQDATIP LIRLGRYFQF NCPRYDNPEL ETRPAIDASS
VLIVKGNNQT VAIQVDRCWG EQEVAIRQVE SNIPLPAGFN NCTILGDGRV LALVNTNDLL
YWIATNQRPP QHNQLPSVRL KTPFIDFKNN KLPAPPTNHK NTILIIDDSI NVRRFLALTL
EKGGYQVEQA KDGQDALEKL ESGLKVAAII CDIEMPRLDG YGFLGRINSN IEMKHIPVTM
LTSRSSNKHR QLAMQLGAQA YFSKPYNEQE LLQTIAELID NVPNTATSN
//
