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
//