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Database: UniProt
Entry: A0A0P7YVM5_9CYAN
LinkDB: A0A0P7YVM5_9CYAN
Original site: A0A0P7YVM5_9CYAN 
ID   A0A0P7YVM5_9CYAN        Unreviewed;       537 AA.
AC   A0A0P7YVM5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HLUCCA11_14480 {ECO:0000313|EMBL:KPQ34502.1};
OS   Phormidesmis priestleyi Ana.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ34502.1, ECO:0000313|Proteomes:UP000050465};
RN   [1] {ECO:0000313|EMBL:KPQ34502.1, ECO:0000313|Proteomes:UP000050465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ana {ECO:0000313|EMBL:KPQ34502.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) 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   -!- 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:KPQ34502.1}.
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DR   EMBL; LJZR01000019; KPQ34502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7YVM5; -.
DR   STRING; 1666911.HLUCCA11_14480; -.
DR   PATRIC; fig|1666911.3.peg.148; -.
DR   Proteomes; UP000050465; Unassembled WGS sequence.
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; cd19410; HK9-like_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KPQ34502.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:KPQ34502.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          259..487
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          225..259
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   537 AA;  59929 MW;  F6D31D8F8571EEA1 CRC64;
     MAGLARRLSH LWQPLPIRVR GAIIIAIPVT CLLTTLSAFA WLKASLAEDE TWIQHTQMVR
     LETKQLANAL VDAETGVRGY GLTQREEFLE PYQSAQVEIP GSLDRLESLV GDNPPQVQQI
     QEIRRLTDDN LTIFQQKLSL KRSLQQISGE PDTKVPAADL YDWLEEGKET MDMARAAIDR
     FTEVEEALLA QRIQHRDRYQ QTAWLALCLL AIISLLAALF AVRLFHQLER ELADREAHLK
     TANHRLENAC NQLQRFTADA SHELRAPLAA VLSNAQVGLM ALDDSEADFL EPADYSSDIR
     SRLENIVSLT KRMSTLVKAL LFLARHESLL AAQDVQRVDL TKLVSQWVVD WQTEVAAHQL
     TLSADLPTVP LTVNANPHLL HQAVTNLFTN AWRYTPAGGH IHLHLYSCKD QAVLEVQDSG
     IGIPKESLSL IFERFYRVDA KRTKATGGLG LGLAIMQQIV QAHRGEVRVT SAVGQGSTFT
     IFLPLEAVDL KTVDSKTVDS KTVDLKTVDL KTVDSKTVDL KTVDLKTVDL KTVDLET
//
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