GLRK_ECOLI
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 03-AUG-2022, entry version 175.
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};
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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 AlphaFoldDB; P52101; -.
DR SMR; P52101; -.
DR BioGRID; 4259204; 3.
DR DIP; DIP-12052N; -.
DR STRING; 511145.b2556; -.
DR jPOST; P52101; -.
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; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_23_6; -.
DR InParanoid; P52101; -.
DR OMA; IAQDCIK; -.
DR PhylomeDB; P52101; -.
DR BioCyc; EcoCyc:G7345-MON; -.
DR BioCyc; MetaCyc:G7345-MON; -.
DR PRO; PR:P52101; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM: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:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IDA:EcoCyc.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0055082; P:cellular chemical homeostasis; IDA:EcoCyc.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; ISM:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0071871; P:response to epinephrine; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; 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
