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Database: UniProt
Entry: K9WTR1_9NOST
LinkDB: K9WTR1_9NOST
Original site: K9WTR1_9NOST 
ID   K9WTR1_9NOST            Unreviewed;       745 AA.
AC   K9WTR1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Cylst_1282 {ECO:0000313|EMBL:AFZ23573.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ23573.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ23573.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ23573.1,
RC   ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-2012) 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};
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DR   EMBL; CP003642; AFZ23573.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9WTR1; -.
DR   STRING; 56107.Cylst_1282; -.
DR   KEGG; csg:Cylst_1282; -.
DR   PATRIC; fig|56107.3.peg.1450; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_032309_0_0_3; -.
DR   Proteomes; UP000010475; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43047:SF82; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE ARLS; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        52..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          242..283
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          317..369
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          370..448
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          443..495
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          499..744
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   745 AA;  84791 MW;  FFD3ACECD6233E8B CRC64;
     MMTTLLKKVQ RWWKKALWTP TTEEVTAVYQ ANLKEKEWLA FRDRFLWQRL HLWLWLGLIC
     LLSFTLRNIY DYFSPLKELV KLPLRTQGLA INFAMLLILL VCFALHKTKF GRRRPGLLFL
     GSSWSISLSS QLFATLKGFA LPDTLGWSLL FLSQATFMPV RWRLHLLSQL VVLVYYFGVN
     WGLRLKTIWP NHPEIYNVTF ILYVFWLCAI CDVGVYLYDC LQRSEFYARR ELESAYQKLE
     TAEVKYRSIF ENAVEGIFQS SSDGRYITAN PALARIYGYS LSEEVTVNFT DIEHQLYVDP
     QRRAEFIRLI EVQGSISEFE SQIYRRDGSI VWISEKAYAV RDEKGNLLYY EGLIEDITQR
     KQAEEALQEQ FNFLQILIDT IPAPVYYKNS QGIYLGCNTA FAASLGLSKG QIIGKSVYDL
     APKDLADQYH QADIALFEQQ QVQSYESSLV YADRTQHDVI FYKATFSKAD GSLGGLVGVI
     LDISTRKRTE EALRVFFHAV SHDLRNPVLG TLMVLRNLLL GGGLGTGGEG RMIEFGSPSS
     IPNTQSLIPV SRSILQRMEQ SGDRQLNLIN SLMEAHKSEV QGVVLQRQPI QLHTVVADAI
     ADLEPMLVEN QATLTNLVTV QLPTVNADSL QLWRVFSNLI VNALKHNPPG LFLQINAINQ
     EDKIYCTVSD NGIGISPEQS VQLFDLYYRS SNIDYVMLRD RNSVSLGLGL YLCKQIINAH
     GGEIGVNTGL ETGVTFWFTL PITAK
//
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