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Database: UniProt
Entry: K9X693_9NOST
LinkDB: K9X693_9NOST
Original site: K9X693_9NOST 
ID   K9X693_9NOST            Unreviewed;      1026 AA.
AC   K9X693;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Chemotaxis protein histidine kinase-like protein {ECO:0000313|EMBL:AFZ27576.1};
GN   ORFNames=Cylst_5568 {ECO:0000313|EMBL:AFZ27576.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ27576.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ27576.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ27576.1,
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.
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DR   EMBL; CP003642; AFZ27576.1; -; Genomic_DNA.
DR   RefSeq; WP_015210811.1; NC_019757.1.
DR   AlphaFoldDB; K9X693; -.
DR   STRING; 56107.Cylst_5568; -.
DR   KEGG; csg:Cylst_5568; -.
DR   PATRIC; fig|56107.3.peg.6129; -.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_295071_0_0_3; -.
DR   Proteomes; UP000010475; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AFZ27576.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475};
KW   Transferase {ECO:0000313|EMBL:AFZ27576.1}.
FT   DOMAIN          2..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   REGION          161..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1026 AA;  112176 MW;  90F2C3AB6473A126 CRC64;
     MLPEQQQRIL GYFLEEARDH LNTIEQGLLN LQSTLNDPEM INEVFRAAHS IKGGAAMLGL
     NSIQHTAHRL EDCFKVLKDN PVQVDEKLES LFLGVSDTLK VLLEHLSGPF GLSEEAANSL
     MSETEPVFRW LNEHLEELVE QGNSGVAITA RATERQLASV NGGTTPTQML PPQNIPNREV
     DTRRPSTETS LNQNWGEFQA TVLQTLREML QLFKQTTTPS TRQNLQQCCH QLSKLGAAHN
     LSHWSGLCQA AASAIANSGA NANTDNSYLN LAKIVITEIK KAQELVLQGR EVEIVISPQL
     NALLSFAEIE LLEITPDFVV EQPQVVAEAA STLEPATADL QPQNSTNSLL DNLKENTGDS
     ASDQLQGTPV TALTATPFAA VPLFDHEEET LLSESNIDTH GPVVGIAELN SLADLFEGDS
     PELDETWHQE EILDTIAANQ LGMGDSDIKD DDKDLADFLS FDDDTSNDHR QTTTSSTEEL
     NLLFGDESFL DRENLEPQNQ PISPASVEVG DITGFNSDLG PSTVEILEEF TVSSSESPQS
     PVEENLLALT LDDNESLPTS EVTSLETENI ASRELPSVSQ SSFDDLESET TNAVPLEELP
     PPQPDSLSLD NLFAELEENT PQPTDESEIG DLFDSPKATA AEVSTSDDEL SNFWNQTNEA
     QPNELDSTVE QDVARDLEES LFAAATSGEI FADSQQSSPS STASFELEDF DITFLQPEQP
     QNLIFASDAG DNLFDDLAGS NSIISPAIGD DEVPLQEIRG FSQEPEALDF IPEFTNLAPE
     TTAADSPKAS ADLEIDLFST VEDDSAENLP LSFDSTYIQP ELTDSEAGEL FGNTLEDDSE
     ENLPLSFDST YIQPELTDSD AGELFGNTLE DDSEENLPLS FDSTYIQPEL TDSEAGELFG
     NSLEDDSEEN LPLSFDSTYI QPELTDSDAG ELFGNSLEED SEENLPLSFD STYIQPELTD
     SEAGELFGNS LEDDSEENLP LSFDSTYIQP ELTDSDAGEL FGNKSGRRQR RKSAAVLWTQ
     LIFNQN
//
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