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Database: UniProt
Entry: A0A3S0Y365_CHLFR
LinkDB: A0A3S0Y365_CHLFR
Original site: A0A3S0Y365_CHLFR 
ID   A0A3S0Y365_CHLFR        Unreviewed;       705 AA.
AC   A0A3S0Y365;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   18-JUN-2025, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PCC6912_18540 {ECO:0000313|EMBL:RUR84260.1};
OS   Chlorogloeopsis fritschii PCC 6912.
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
OC   Chlorogloeopsidaceae; Chlorogloeopsis.
OX   NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR84260.1, ECO:0000313|Proteomes:UP000268857};
RN   [1] {ECO:0000313|EMBL:RUR84260.1, ECO:0000313|Proteomes:UP000268857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR84260.1,
RC   ECO:0000313|Proteomes:UP000268857};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2019).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUR84260.1}.
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DR   EMBL; RSCJ01000005; RUR84260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0Y365; -.
DR   STRING; 211165.GCA_000317285_00740; -.
DR   Proteomes; UP000268857; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 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   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268857};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          308..360
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          432..690
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          361..423
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   705 AA;  77502 MW;  77272098A5593540 CRC64;
     MLVNQARSEL AVTEINYNIK INQMGFGFRG QSDNAAIIAA AKAHANSQRL DSTLQRQVKQ
     ILQNEVKARE IEYATLVGKD LRIIVNANAD RIGEIFNPSN LVGEVLKNPQ QIKTSEIVSR
     AELAKEKPPL PVGIEGYDAL IRYTVTPVRN PQTQEVLGAL VSGDIVNDKP PIVHQTVVTL
     GGGYSAVYSR QPNGEFALAT AEQDTNTDKQ GQENQGVRYV SLPDTALLSA AVEARGKPVT
     QRIAVEGQTY TVAARALLNF AGETVAILVR GTPETALNAL LRQSLLLQGG IAVLALSVDV
     LLATLLARAI ARPIGHLQQV TQAFSGGNFQ ARAQVLSADE IGQLAATFNQ MADSIVSTWQ
     IEAIAQEQAR LNAQLQQEIA ERTRTEEALQ QSETLLREKN QILEQTLAQL RSTQAQMVQA
     EKMSSLGQLV AGVAHEINNP VNFIHGNLTH AHQYTQDLMG LIQLYQQHYL NPPQAIQAEI
     EAIELDFLIE DLIKLFKSMQ VGTERIQEIV LSLRNFSRLD EAEFKAVNIH EGIDSTLMIL
     GNRLKAKPEH SSIEIIKNYG QLPSVECYPG QLNQVFMNLL TNAIDALEEH NRQRSPQEIK
     ANPGTIRIST EMIEADWIAI YIADNGLGMT EEVRSRIFDS FFITKPIGKG TGLGLSISYE
     IVTEKHGGKL YCHSTPGQGT EFVIELPVRQ QIHAPHNLMR SVASV
//
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