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Database: UniProt
Entry: A0A0N7Z3J8_9CYAN
LinkDB: A0A0N7Z3J8_9CYAN
Original site: A0A0N7Z3J8_9CYAN 
ID   A0A0N7Z3J8_9CYAN        Unreviewed;       459 AA.
AC   A0A0N7Z3J8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NIES2104_00110 {ECO:0000313|EMBL:GAP93505.1};
OS   Leptolyngbya sp. NIES-2104.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP93505.1, ECO:0000313|Proteomes:UP000052243};
RN   [1] {ECO:0000313|EMBL:GAP93505.1, ECO:0000313|Proteomes:UP000052243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP93505.1,
RC   ECO:0000313|Proteomes:UP000052243};
RX   PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA   Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA   Kawachi M.;
RT   "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT   and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL   DNA Res. 22:403-412(2015).
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:GAP93505.1}.
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DR   EMBL; BBWW01000001; GAP93505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N7Z3J8; -.
DR   STRING; 1552121.NIES2104_00110; -.
DR   InParanoid; A0A0N7Z3J8; -.
DR   Proteomes; UP000052243; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
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; 1.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          91..139
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          164..216
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          237..456
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          64..98
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   459 AA;  52393 MW;  72503B19042BD0E8 CRC64;
     MLTLLENLDR SVMNESENTR DRQKLIQQLE AVDQQVHQLF ESVDHYSSPD ASFSEYLSAL
     SKALEELKLT EEQICQQNQQ LSEARQALEI EQQRYQELFE FAPDGYLITD NHGTIQEANR
     VAVDLLKIDK KYIVGKTLIN FVGEGHRHVF RLLLLQLQSI NQVREWEIPM VAQDGTQFVA
     ALTTVAVRTE SGDTIALRWL IRDITTRKQI EEQLRKIQHQ NLQLIEADRL KEQFIATMSH
     ELRTPLTAIL GFSDLLLRQF HRQFPPHQTK LIERIFENGR HLLSLIEDIL DFSNLRAKRI
     ELQLEMFDLN ELVGHTVEEM RSMAEQKKLS IHTHFSTTDP LILNDRSRVK QILVNLISNA
     IKFTDSGSVC VQVKSGKFGR IAIVVQDTGI GIDDNNLDTI FQEFRQVNQT STRQHGGTGL
     GLAITKALTQ LMGGEITVQS KLGSGSTFTV ELPMRLASL
//
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