ID Q7NL87_GLOVI Unreviewed; 713 AA.
AC Q7NL87;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=glr1239 {ECO:0000313|EMBL:BAC89180.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC89180.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC89180.1, 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000045; BAC89180.1; -; Genomic_DNA.
DR RefSeq; NP_924185.1; NC_005125.1.
DR RefSeq; WP_011141239.1; NC_005125.1.
DR AlphaFoldDB; Q7NL87; -.
DR STRING; 251221.gene:10758720; -.
DR EnsemblBacteria; BAC89180; BAC89180; BAC89180.
DR KEGG; gvi:glr1239; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR InParanoid; Q7NL87; -.
DR OrthoDB; 9790669at2; -.
DR PhylomeDB; Q7NL87; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 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:BAC89180.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW Transferase {ECO:0000313|EMBL:BAC89180.1}.
FT DOMAIN 21..91
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 159..215
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 232..284
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 491..708
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 128..162
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 464..491
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 713 AA; 79073 MW; 1243CE843C8EB41F CRC64;
MDELLVDNGT DGGHRRALEQ SELRYRQLVE LSPDAIFVQC EGKVVFINGA GGRLLGAETS
AQIVGKPVLE LIHPCDREAV RRRMELLQAG TAVPLLEERF LRLDGTVVEV EVLASAMTYQ
GKPAAHVLAR DIGERKRAQH EREQLLERRR QALATAEQSE ERYRLLIEAI PQLVWTTTAD
GRCDYLSQQW VHYTGIPEAE QLGMGWLAAV HPEDRPRASA CWLAAVADRA IYDLEYRLRA
ADGSYRWFKT RGRPVRDAGG RIVRWFGTCT DMQDQKTAQE ERERLIAHQQ QYAARLKKLS
EASLAINLAL SVEEVVEVIT FQASAIIGTH QAVTSMTIDA DWGRAINAVY LSEKYAAWRD
FRGRPNGAAI YARVCDTNRP MRLNQAQLDA HPHWRTFGNA DTEHPPLRGW LAAPLVARDG
RNIGLIQLSD KCEEEFTAED EAIVVQLAQM ASVAIENARL FEAEQTARAL AEQARREAEA
ANRAKDEFLA VLSHELRTPL NPIIGFAQLL RRKSGLSAAD YRALETIERN GRLQAQLIDD
VLDVSRIISG KMRVELRAVD LLPVVAAAIE AVRSPAELKG ICLSGRLDDG ATAVADPTRM
QQVVWNLLTN AIKFTPEGGR VVIDLCRGDR TLLIRVSDSG IGISPDFLPY VFERFRQADG
TSTRKHSGLG LGLAIVRHIV ELHGGAVSAQ SDGVGQGTTF CVELPLYTCE PTA
//
