ID K9WTV1_9NOST Unreviewed; 443 AA.
AC K9WTV1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cylst_0641 {ECO:0000313|EMBL:AFZ22972.1};
OS Cylindrospermum stagnale PCC 7417.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Cylindrospermum.
OX NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ22972.1, ECO:0000313|Proteomes:UP000010475};
RN [1] {ECO:0000313|EMBL:AFZ22972.1, ECO:0000313|Proteomes:UP000010475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ22972.1,
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; AFZ22972.1; -; Genomic_DNA.
DR AlphaFoldDB; K9WTV1; -.
DR STRING; 56107.Cylst_0641; -.
DR KEGG; csg:Cylst_0641; -.
DR PATRIC; fig|56107.3.peg.714; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_6_3; -.
DR Proteomes; UP000010475; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ22972.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010475};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..220
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 228..442
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 443 AA; 49541 MW; 7B7BEAB40DBE75A7 CRC64;
MAGYILWSFY AYFMRSRQMD LDNWTNALSQ SAADALAEQN LQKVEVLVQR YGAPQNVTLR
IFNQQGRLLA TSDPNGDKKV TNWYQVSGVS AALQNRIEQG FSKGVLTNED RLYVARPIVR
DGQLLGVVRL SITLNQVQNQ FTRVIWSVLG TLALTILLCA LISTRFARSL SKPIETMRNF
AIRLGSGHFG DKLEIHENNE LDQLATELNR MSERLASLDQ ERRVFLANVS HELRTPISNV
QVTVDALRSG AYEEPELRDR FFQTIENEIK RLSRLIHDLL DLGRLEAGVY QLEQQPISLL
GLINRAVGAM EPRMQTIGIS ARVNVVDLLI QGDPERLLQA VLNVLDNAIK HSLPNSQIFI
SGYNEGNLAV VRIKDQGTGI SEHDLPRIFE QFYTTNPSRQ GNGNGLGLAI AKRIIEAHHG
SITASSTANQ GAIFTICLPL KVR
//