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ECOLI:LRP

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) lrp (synonyms: alsB, ihb, livR, oppI)
Protein Name(s) Leucine-responsive regulatory protein
External Links
UniProt P0ACJ0
EMBL M35869
D11105
U00096
AP009048
PIR JH0412
RefSeq NP_415409.1
YP_489161.1
PDB 2GQQ
2L4A
PDBsum 2GQQ
2L4A
ProteinModelPortal P0ACJ0
SMR P0ACJ0
DIP DIP-35825N
IntAct P0ACJ0
STRING 511145.b0889
PaxDb P0ACJ0
PRIDE P0ACJ0
EnsemblBacteria AAC73975
BAA35614
GeneID 12931703
949051
KEGG ecj:Y75_p0861
eco:b0889
PATRIC 32116989
EchoBASE EB0542
EcoGene EG10547
eggNOG COG1522
HOGENOM HOG000115327
InParanoid P0ACJ0
KO K03719
OMA LVFVEIK
OrthoDB EOG6F29D2
PhylomeDB P0ACJ0
BioCyc EcoCyc:PD00353
ECOL316407:JW0872-MONOMER
EvolutionaryTrace P0ACJ0
PRO PR:P0ACJ0
Proteomes UP000000318
UP000000625
Genevestigator P0ACJ0
GO GO:0005622
GO:0042802
GO:0043565
GO:0003700
GO:0009098
GO:0006355
GO:0043201
GO:0006351
Gene3D 1.10.10.10
3.30.70.920
InterPro IPR000485
IPR011008
IPR019888
IPR019887
IPR019885
IPR011991
Pfam PF01037
PF13412
PRINTS PR00033
SMART SM00344
SUPFAM SSF54909
PROSITE PS00519
PS50956

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0010467

gene expression

PMID:8955316[1]

ECO:0000269

P

Figure 1B indicates that the induction of of lrp expression in cells entering the stationary phase, grown in a rich medium, is not dependent on the stationary phase sigma factor encoded by rpoS

complete

GO:0010467

gene expression

PMID:8955316[1]

ECO:0000269

P

Table 2 illustrates that Lrp does not play any role in the stationary phase induction of the lrp gene.

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:8144448[2]

ECO:0005657

primer extension assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:8144448[2]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:10216857[3]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:10216857[3]

ECO:0005643

hydroxyl-radical footprinting evidence used in manual assertion

RefSeq:NC_000913.2

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:8144448[2]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.2

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:8144448[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:8144448[2]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:10216857[3]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:10216857[3]

ECO:0005643

hydroxyl-radical footprinting evidence used in manual assertion

RefSeq:NC_000913.2

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:8144448[2]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.2

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:8144448[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001216

DNA-binding transcription activator activity

PMID:10216857[3]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001216

DNA-binding transcription activator activity

PMID:10216857[3]

ECO:0005643

hydroxyl-radical footprinting evidence used in manual assertion

RefSeq:NC_000913.2

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:8144448[2]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:10216857[3]

ECO:0005667

site-directed mutagenesis phenotypic evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:10216857[3]

ECO:0005643

hydroxyl-radical footprinting evidence used in manual assertion

RefSeq:NC_000913.2

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:8144448[2]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.2

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:8144448[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10547
PANTHER:PTN001248975

F

Seeded From UniProt

complete

involved_in

GO:0043201

response to leucine

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10547
PANTHER:PTN000765740

P

Seeded From UniProt

complete

involved_in

GO:0006524

alanine catabolic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000765740
UniProtKB:Q9HTP6

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10547
PANTHER:PTN001248975

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21642464[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACJ0

F

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:10551881[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043201

response to leucine

PMID:12054800[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

PMID:12374860[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009098

leucine biosynthetic process

PMID:12054800[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001216

P

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001216

P

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR019888

F

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR019888

P

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000485
InterPro:IPR019888

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Landgraf, JR et al. (1996) Effects of nutrition and growth rate on Lrp levels in Escherichia coli. J. Bacteriol. 178 6930-6 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 2.9 Wang, Q et al. (1994) Regulation of the Escherichia coli lrp gene. J. Bacteriol. 176 1831-9 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 Zhi, J et al. (1999) Lrp binds to two regions in the dadAX promoter region of Escherichia coli to repress and activate transcription directly. Mol. Microbiol. 32 29-40 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. Hart, BR et al. (2011) Recognition of DNA by the helix-turn-helix global regulatory protein Lrp is modulated by the amino terminus. J. Bacteriol. 193 3794-803 PubMed GONUTS page
  6. Azam, TA & Ishihama, A (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274 33105-13 PubMed GONUTS page
  7. 7.0 7.1 Chen, S & Calvo, JM (2002) Leucine-induced dissociation of Escherichia coli Lrp hexadecamers to octamers. J. Mol. Biol. 318 1031-42 PubMed GONUTS page
  8. Tani, TH et al. (2002) Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis. Proc. Natl. Acad. Sci. U.S.A. 99 13471-6 PubMed GONUTS page
  9. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page