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Database: UniProt
Entry: Q7NK92_GLOVI
LinkDB: Q7NK92_GLOVI
Original site: Q7NK92_GLOVI 
ID   Q7NK92_GLOVI            Unreviewed;       411 AA.
AC   Q7NK92;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=glr1586 {ECO:0000313|EMBL:BAC89527.1};
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC89527.1, ECO:0000313|Proteomes:UP000000557};
RN   [1] {ECO:0000313|EMBL:BAC89527.1, ECO:0000313|Proteomes:UP000000557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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};
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DR   EMBL; BA000045; BAC89527.1; -; Genomic_DNA.
DR   RefSeq; NP_924532.1; NC_005125.1.
DR   RefSeq; WP_011141585.1; NC_005125.1.
DR   AlphaFoldDB; Q7NK92; -.
DR   STRING; 251221.gene:10759075; -.
DR   EnsemblBacteria; BAC89527; BAC89527; BAC89527.
DR   KEGG; gvi:glr1586; -.
DR   PATRIC; fig|251221.4.peg.1623; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_672262_0_0_3; -.
DR   InParanoid; Q7NK92; -.
DR   OrthoDB; 537027at2; -.
DR   PhylomeDB; Q7NK92; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00512; 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   Kinase {ECO:0000313|EMBL:BAC89527.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW   Transferase {ECO:0000313|EMBL:BAC89527.1}.
FT   DOMAIN          199..411
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   411 AA;  44730 MW;  AFA3F86D6D87672B CRC64;
     METLGLAPRL RSLSQALAAG PPFAEQLQAA GSRTWSMAVA ALAGFLGEHP ARVILFAGGK
     FDLAALSAVG TVAPKLWQFQ TLLAHKPQGE VVVPLSAGDP LADENFLVVI AHDFCLVLCH
     RSPTLQFSFE TAVVRRACTV LRQRLVITRP DRLAAFDRAL SHPPLASVRL LSRFSRALLA
     EGSRAQESID GSELDFLELL AHEVRTPLTT IRTLTRLVLR KGGLTESART HLEAIDRECA
     LQIERFELLA LAMDHEQGEL ALRPQAVAVD ELLMGCLERW REQADLRGLA LDVDPPAELP
     RVHADQLLLE RVLGGLVDRL VRSLPFGSHI QLKAERAGFW LRVRIDITGG SVENPSAEDA
     NPFRVDSQAG AVTLRLPAAQ GLVAAMGGKL TLRLRPEGES STLTLYLPIQ S
//
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