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Database: UniProt
Entry: A0A218QRS6_9CYAN
LinkDB: A0A218QRS6_9CYAN
Original site: A0A218QRS6_9CYAN 
ID   A0A218QRS6_9CYAN        Unreviewed;       713 AA.
AC   A0A218QRS6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NIES4075_56880 {ECO:0000313|EMBL:GAX44669.1};
OS   Tolypothrix sp. NIES-4075.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX44669.1, ECO:0000313|Proteomes:UP000198313};
RN   [1] {ECO:0000313|EMBL:GAX44669.1, ECO:0000313|Proteomes:UP000198313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX44669.1,
RC   ECO:0000313|Proteomes:UP000198313};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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:GAX44669.1}.
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DR   EMBL; BDUC01000008; GAX44669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218QRS6; -.
DR   OrthoDB; 524708at2; -.
DR   Proteomes; UP000198313; 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   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; 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
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   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
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; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GAX44669.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198313};
KW   Transferase {ECO:0000313|EMBL:GAX44669.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          222..286
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          346..419
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          420..472
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          489..705
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          205..232
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   713 AA;  82729 MW;  57D5BF43E5149FFF CRC64;
     MKWSLERKII AVGFGLAVLI IAIVNIISYQ NTEKLFVRER QLEYSYEVIQ KARDVLTTVR
     DAEKARRSYI TTGNNSYLET YNTAIQSIEA KLTDAQRAIS GSPTQQQKLD ILKPLIAQRV
     SLLKQSVDFY KRDKSNTAIQ LALTDKSITI QDQIWQIITQ IEKEEQSLVQ RHQVRSDASF
     RFTIVAQITG YWISFALLFI VYSLLHRQIS TRQQLEDTLR ESQQRYRNLF EVNPHPLWVY
     DLENLNFLAV NEVAIKQYGY SQSEFLSMTI KDIRPPEEVP ALLDRIPGLR WADKRFATRR
     HKKRDGTEID VEIISHELTF KGRPARLVLA RDITQQKQAQ EALAASEEKF RQIAENINEI
     FWMRDAKADI VLYVNPAYER IWGRSCESLY INPQSFLDAV HPEDKSRVIA NLENNIKKEF
     EIEYRIVRPD DSVRWVWEHS FPIKNRLGKV YRRAVVTQDI TERKRAEEVQ RNLEKELELN
     ELKIRFFSMV SHEFRTPLST ILISAQLLEN SNKEWSEEKK LKNLHRIQSS AKTMTQLLTD
     ILTLTRAEAG KLEFRPQPLD LEEFCFSLLE EIKFSTRAEK DIVFVSECSQ RIAWMDERML
     RSIVTNLVDN AIKYSPDDSQ IYFTLAAESG QAIFQIQDQG IGICQEEEEQ LYQAFQRGEN
     VGDVTGTGLG LAVVKKCVEL HGGNIKLESK VGVGTTFTVR IPWKSDLGEV KRC
//
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