GLRR_ECOLI
ID GLRR_ECOLI Reviewed; 444 AA.
AC P0AFU4; P21712; P77512;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transcriptional regulatory protein GlrR;
GN Name=glrR; Synonyms=yfhA; OrderedLocusNames=b2554, JW2538;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8226691; DOI=10.1128/jb.175.22.7441-7449.1993;
RA Liu J., Magasanik B.;
RT "The glnB region of the Escherichia coli chromosome.";
RL J. Bacteriol. 175:7441-7449(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-444.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8412694; DOI=10.1111/j.1365-2958.1993.tb01706.x;
RA van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
RT "The genes of the glutamine synthetase adenylylation cascade are not
RT regulated by nitrogen in Escherichia coli.";
RL Mol. Microbiol. 9:443-458(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 404-444.
RC STRAIN=K12;
RX PubMed=2034230; DOI=10.1007/bf00273586;
RA Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E.,
RA Poole R.K.;
RT "Isolation and nucleotide sequence of the hmp gene that encodes a
RT haemoglobin-like protein in Escherichia coli K-12.";
RL Mol. Gen. Genet. 226:49-58(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-444.
RX PubMed=2885322; DOI=10.1016/s0021-9258(18)47469-8;
RA Son H.S., Rhee S.G.;
RT "Cascade control of Escherichia coli glutamine synthetase. Purification and
RT properties of PII protein and nucleotide sequence of its structural gene.";
RL J. Biol. Chem. 262:8690-8695(1987).
RN [8]
RP PHOSPHORYLATION.
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 [9]
RP FUNCTION, DNA-BINDING, 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. Regulates glmY transcription by binding to
CC three conserved sites in the purL-glmY intergenic region.
CC {ECO:0000269|PubMed:19843219}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by GlrK. {ECO:0000269|PubMed:15522865}.
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=AAA79816.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S67014; AAB28778.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75607.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16462.1; -; Genomic_DNA.
DR EMBL; Z21843; CAA79889.1; -; Genomic_DNA.
DR EMBL; M16778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U36841; AAA79816.1; ALT_INIT; Genomic_DNA.
DR PIR; A65033; A65033.
DR RefSeq; NP_417049.1; NC_000913.3.
DR RefSeq; WP_001295369.1; NZ_LN832404.1.
DR AlphaFoldDB; P0AFU4; -.
DR SMR; P0AFU4; -.
DR BioGRID; 4259202; 1.
DR BioGRID; 851381; 2.
DR DIP; DIP-12044N; -.
DR IntAct; P0AFU4; 9.
DR STRING; 511145.b2554; -.
DR iPTMnet; P0AFU4; -.
DR jPOST; P0AFU4; -.
DR PaxDb; P0AFU4; -.
DR PRIDE; P0AFU4; -.
DR EnsemblBacteria; AAC75607; AAC75607; b2554.
DR EnsemblBacteria; BAA16462; BAA16462; BAA16462.
DR GeneID; 947042; -.
DR KEGG; ecj:JW2538; -.
DR KEGG; eco:b2554; -.
DR PATRIC; fig|1411691.4.peg.4180; -.
DR EchoBASE; EB1262; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR InParanoid; P0AFU4; -.
DR OMA; YRAVVMS; -.
DR PhylomeDB; P0AFU4; -.
DR BioCyc; EcoCyc:EG11285-MON; -.
DR PRO; PR:P0AFU4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IMP:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IMP:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..444
FT /note="Transcriptional regulatory protein GlrR"
FT /id="PRO_0000081377"
FT DOMAIN 7..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 136..366
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 414..433
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 227..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 106
FT /note="K -> N (in Ref. 1; AAB28778)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..310
FT /note="ER -> DG (in Ref. 1; AAB28778)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..328
FT /note="ER -> DG (in Ref. 1; AAB28778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 49148 MW; 6553C027DE5513EF CRC64;
MSHKPAHLLL VDDDPGLLKL LGLRLTSEGY SVVTAESGAE GLRVLNREKV DLVISDLRMD
EMDGMQLFAE IQKVQPGMPV IILTAHGSIP DAVAATQQGV FSFLTKPVDK DALYQAIDDA
LEQSAPATDE RWREAIVTRS PLMLRLLEQA RLVAQSDVSV LINGQSGTGK EIFAQAIHNA
SPRNSKPFIA INCGALPEQL LESELFGHAR GAFTGAVSNR EGLFQAAEGG TLFLDEIGDM
PAPLQVKLLR VLQERKVRPL GSNRDIDINV RIISATHRDL PKAMARGEFR EDLYYRLNVV
SLKIPALAER TEDIPLLANH LLRQAAERHK PFVRAFSTDA MKRLMTASWP GNVRQLVNVI
EQCVALTSSP VISDALVEQA LEGENTALPT FVEARNQFEL NYLRKLLQIT KGNVTHAARM
AGRNRTEFYK LLSRHELDAN DFKE
