GLAR_ECOLI
ID GLAR_ECOLI Reviewed; 220 AA.
AC P37338; P76623; P77021;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=HTH-type transcriptional repressor GlaR;
DE AltName: Full=Carbon starvation induced regulator;
DE AltName: Full=GlaH operon repressor {ECO:0000305|PubMed:30498244};
GN Name=glaR {ECO:0000303|PubMed:30498244}; Synonyms=csiR, gabC, ygaE;
GN OrderedLocusNames=b2664, JW2639;
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 / 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RC STRAIN=K12 / JM103 / ATCC 39403 / DSM 2829 / KCTC 1112 / NCIMB 12044;
RX PubMed=8297211; DOI=10.1007/bf00245306;
RA Niegemann E., Schulz A., Bartsch K.;
RT "Molecular organization of the Escherichia coli gab cluster: nucleotide
RT sequence of the structural genes gabD and gabP and expression of the GABA
RT permease gene.";
RL Arch. Microbiol. 160:454-460(1993).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14731280; DOI=10.1046/j.1365-2958.2003.03867.x;
RA Metzner M., Germer J., Hengge R.;
RT "Multiple stress signal integration in the regulation of the complex sigma
RT S-dependent csiD-ygaF-gabDTP operon in Escherichia coli.";
RL Mol. Microbiol. 51:799-811(2004).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND DNA-BINDING.
RC STRAIN=K12 / BW25113;
RX PubMed=30498244; DOI=10.1038/s41467-018-07563-6;
RA Knorr S., Sinn M., Galetskiy D., Williams R.M., Wang C., Mueller N.,
RA Mayans O., Schleheck D., Hartig J.S.;
RT "Widespread bacterial lysine degradation proceeding via glutarate and L-2-
RT hydroxyglutarate.";
RL Nat. Commun. 9:5071-5071(2018).
CC -!- FUNCTION: Negatively regulates the expression of the glaH-lhgD-gabDTP
CC operon in a temporal manner during entry into stationary phase or
CC during the first few hours of carbon starvation (PubMed:14731280,
CC PubMed:30498244). Thereby is involved in the regulation of a L-lysine
CC degradation pathway that proceeds via cadaverine, glutarate and L-2-
CC hydroxyglutarate (PubMed:30498244). Binds to two primary and two
CC secondary sites in the promoter region of the glaH operon with the
CC consensus sequences TTGTN5TTTT and ATGTN5TTTT of the primary sites,
CC each separated by six nucleotides (PubMed:30498244).
CC {ECO:0000269|PubMed:14731280, ECO:0000269|PubMed:30498244}.
CC -!- ACTIVITY REGULATION: The repressive effect at the glaH promoter site is
CC specifically relieved upon glutarate binding.
CC {ECO:0000269|PubMed:30498244}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; U00096; AAC75711.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16527.1; -; Genomic_DNA.
DR EMBL; M88334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_417150.4; NC_000913.3.
DR RefSeq; WP_000156811.1; NZ_STEB01000042.1.
DR AlphaFoldDB; P37338; -.
DR SMR; P37338; -.
DR BioGRID; 4262265; 4.
DR DIP; DIP-12095N; -.
DR IntAct; P37338; 4.
DR STRING; 511145.b2664; -.
DR jPOST; P37338; -.
DR PaxDb; P37338; -.
DR PRIDE; P37338; -.
DR EnsemblBacteria; AAC75711; AAC75711; b2664.
DR EnsemblBacteria; BAA16527; BAA16527; BAA16527.
DR GeneID; 66673466; -.
DR GeneID; 948055; -.
DR KEGG; ecj:JW2639; -.
DR KEGG; eco:b2664; -.
DR PATRIC; fig|1411691.4.peg.4077; -.
DR EchoBASE; EB2287; -.
DR eggNOG; COG1802; Bacteria.
DR HOGENOM; CLU_017584_5_3_6; -.
DR InParanoid; P37338; -.
DR OMA; RYRHLWL; -.
DR PhylomeDB; P37338; -.
DR BioCyc; EcoCyc:EG12386-MON; -.
DR PRO; PR:P37338; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.120.530; -; 1.
DR InterPro; IPR011711; GntR_C.
DR InterPro; IPR008920; TF_FadR/GntR_C.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF07729; FCD; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00895; FCD; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48008; SSF48008; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..220
FT /note="HTH-type transcriptional repressor GlaR"
FT /id="PRO_0000050680"
FT DOMAIN 1..69
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 29..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
SQ SEQUENCE 220 AA; 24991 MW; C86A1AE9F767D092 CRC64;
MTITSLDGYR WLKNDIIRGN FQPDEKLRMS LLTSRYALGV GPLREALSQL VAERLVTVVN
QKGYRVASMS EQELLDIFDA RANMEAMLVS LAIARGGDEW EADVLAKAHL LSKLEACDAS
EKMLDEWDLR HQAFHTAIVA GCGSHYLLQM RERLFDLAAR YRFIWLRRTV LSVEMLEDKH
DQHQTLTAAV LARDTARASE LMRQHLLTPI PIIQQAMAGN
