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};
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; 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
//