ID GLRK_ECOLI Reviewed; 475 AA. AC P52101; P76587; Q2MAH4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 3. DT 26-FEB-2020, entry version 164. DE RecName: Full=Sensor histidine kinase GlrK; DE EC=2.7.13.3; GN Name=glrK; Synonyms=yfhK; OrderedLocusNames=b2556, JW5407; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [3] RP FUNCTION, AND AUTOPHOSPHORYLATION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=15522865; DOI=10.1074/jbc.m410104200; RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.; RT "Functional characterization in vitro of all two-component signal RT transduction systems from Escherichia coli."; RL J. Biol. Chem. 280:1448-1456(2005). RN [4] RP TOPOLOGY [LARGE SCALE ANALYSIS]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). RN [5] RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME. RX PubMed=19843219; DOI=10.1111/j.1365-2958.2009.06918.x; RA Reichenbach B., Gopel Y., Gorke B.; RT "Dual control by perfectly overlapping sigma 54- and sigma 70-promoters RT adjusts small RNA GlmY expression to different environmental signals."; RL Mol. Microbiol. 74:1054-1070(2009). CC -!- FUNCTION: Member of the two-component regulatory system GlrR/GlrK that CC up-regulates transcription of the glmY sRNA when cells enter the CC stationary growth phase. Activates GlrR by phosphorylation. CC {ECO:0000269|PubMed:15522865, ECO:0000269|PubMed:19843219}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. CC -!- PTM: Autophosphorylated. CC -!- DISRUPTION PHENOTYPE: Mutants show decreased amounts of glmY. CC {ECO:0000269|PubMed:19843219}. CC -!- MISCELLANEOUS: Not required for the regulation of the glmY-glmZ-glmS CC regulatory cascade by glucosamine-6-phosphate depletion. CC -!- SEQUENCE CAUTION: CC Sequence=AAA79818.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; U36841; AAA79818.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC75609.2; -; Genomic_DNA. DR EMBL; AP009048; BAE76732.1; -; Genomic_DNA. DR PIR; C65033; C65033. DR RefSeq; NP_417051.2; NC_000913.3. DR RefSeq; WP_001311037.1; NZ_LN832404.1. DR SMR; P52101; -. DR BioGrid; 4259204; 3. DR DIP; DIP-12052N; -. DR STRING; 511145.b2556; -. DR PaxDb; P52101; -. DR PRIDE; P52101; -. DR EnsemblBacteria; AAC75609; AAC75609; b2556. DR EnsemblBacteria; BAE76732; BAE76732; BAE76732. DR GeneID; 947013; -. DR KEGG; ecj:JW5407; -. DR KEGG; eco:b2556; -. DR PATRIC; fig|511145.12.peg.2658; -. DR EchoBASE; EB3234; -. DR eggNOG; ENOG4107WP9; Bacteria. DR eggNOG; ENOG410Y4CW; LUCA. DR HOGENOM; CLU_000445_89_23_6; -. DR InParanoid; P52101; -. DR KO; K07711; -. DR PhylomeDB; P52101; -. DR BioCyc; EcoCyc:G7345-MONOMER; -. DR BioCyc; ECOL316407:JW5407-MONOMER; -. DR PRO; PR:P52101; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc. DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central. DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central. DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc. DR GO; GO:0071871; P:response to epinephrine; IDA:EcoCyc. DR GO; GO:0023014; P:signal transduction by protein phosphorylation; IDA:EcoCyc. DR CDD; cd00082; HisKA; 1. DR Gene3D; 3.30.565.10; -; 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; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix; Two-component regulatory system. FT CHAIN 1..475 FT /note="Sensor histidine kinase GlrK" FT /id="PRO_0000074915" FT TOPO_DOM 1..13 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 14..34 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 35..173 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 174..194 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 195..475 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 256..472 FT /note="Histidine kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT MOD_RES 259 FT /note="Phosphohistidine; by autocatalysis" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" SQ SEQUENCE 475 AA; 53330 MW; EBB3F4D821C24AEB CRC64; MKRWPVFPRS LRQLVMLAFL LILLPLLVLA WQAWQSLNAL SDQAALVNRT TLIDARRSEA MTNAALEMER SYRQYCVLDD PTLAKVYQSQ RKRYSEMLDA HAGVLPDDKL YQALRQDLHN LAQLQCNNSG PDAAAAARLE AFASANTEMV QATRTVVFSR GQQLQREIAE RGQYFGWQSL VLFLVSLVMV LLFTRMIIGP VKNIERMINR LGEGRSLGNS VSFSGPSELR SVGQRILWLS ERLSWLESQR HQFLRHLSHE LKTPLASMRE GTELLADQVV GPLTPEQKEV VSILDSSSRN LQKLIEQLLD YNRKQADSAV ELENVELAPL VETVVSAHSL PARAKMMHTD VDLKATACLA EPMLLMSVLD NLYSNAVHYG AESGNICLRS SLHGARVYID VINTGTPIPQ EERAMIFEPF FQGSHQRKGA VKGSGLGLSI ARDCIRRMQG ELYLVDESGQ DVCFRIELPS SKNTK //