GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ECOLI:CRP

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) crp (synonyms: cap, csm)
Protein Name(s) cAMP-activated global transcriptional regulator CRP

Catabolite activator protein CAP Catabolite gene activator cAMP receptor protein CRP cAMP regulatory protein

External Links
UniProt P0ACJ8
EMBL J01598
U18997
U00096
AP009048
PIR A93416
RefSeq NP_417816.1
YP_492074.1
PDB 1CGP
1G6N
1HW5
1I5Z
1I6X
1J59
1LB2
1O3Q
1O3R
1O3S
1O3T
1RUN
1RUO
1ZRC
1ZRD
1ZRE
1ZRF
2CGP
2GAP
2GZW
2WC2
3FWE
3HIF
3IYD
3KCC
3N4M
3QOP
3RDI
3ROU
3RPQ
3RYP
3RYR
4BH9
4BHP
4FT8
4HZF
4I01
4I02
4I09
4I0A
4I0B
PDBsum 1CGP
1G6N
1HW5
1I5Z
1I6X
1J59
1LB2
1O3Q
1O3R
1O3S
1O3T
1RUN
1RUO
1ZRC
1ZRD
1ZRE
1ZRF
2CGP
2GAP
2GZW
2WC2
3FWE
3HIF
3IYD
3KCC
3N4M
3QOP
3RDI
3ROU
3RPQ
3RYP
3RYR
4BH9
4BHP
4FT8
4HZF
4I01
4I02
4I09
4I0A
4I0B
ProteinModelPortal P0ACJ8
SMR P0ACJ8
DIP DIP-29232N
IntAct P0ACJ8
MINT MINT-1249660
STRING 511145.b3357
PaxDb P0ACJ8
PRIDE P0ACJ8
EnsemblBacteria AAC76382
BAE77933
GeneID 12933934
947867
KEGG ecj:Y75_p3818
eco:b3357
PATRIC 32122148
EchoBASE EB0162
EcoGene EG10164
eggNOG COG0664
HOGENOM HOG000250565
InParanoid P0ACJ8
KO K10914
OMA RAKSACE
OrthoDB EOG69GZGV
PhylomeDB P0ACJ8
BioCyc EcoCyc:PD00257
ECOL316407:JW5702-MONOMER
EvolutionaryTrace P0ACJ8
PRO PR:P0ACJ8
Proteomes UP000000318
UP000000625
Genevestigator P0ACJ8
GO GO:0005622
GO:0030552
GO:0003677
GO:0003700
GO:0045013
GO:0045892
GO:0045893
GO:0006351
Gene3D 1.10.10.10
2.60.120.10
InterPro IPR018490
IPR018488
IPR000595
IPR012318
IPR014710
IPR001808
IPR018335
IPR011991
Pfam PF00027
PF00325
PRINTS PR00034
SMART SM00100
SM00419
SUPFAM SSF51206
PROSITE PS00888
PS00889
PS50042
PS00042
PS51063

Annotations

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

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

PMID:15150239[1]

ECO:0001808

reverse transcription polymerase chain reaction evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:15150239[1]

ECO:0001808

reverse transcription polymerase chain reaction evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:9202484[2]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.2

F

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:9202484[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:9202484[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:9202484[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10164
EcoGene:EG10325
PANTHER:PTN000705815

C

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10325
PANTHER:PTN000705815
UniProtKB:P22260
UniProtKB:P46148
UniProtKB:P9WMH3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23644478[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACJ8

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19805344[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACJ8

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19359484[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACJ8

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16906160[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACJ8

F

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

PMID:15520470[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:15520470[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045013

carbon catabolite repression of transcription

PMID:16838379[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:8604346[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:12923087[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:7551052[12]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:16166533[13]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:12923087[11]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:11742992[14]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:10760178[15]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:7551052[12]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:15520470[8]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:6343617[16]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P0A9E5

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[17]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012318

F

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:IPR018335

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:IPR012318
InterPro:IPR018335

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

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

enables

GO:0030552

cAMP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0116

F

Seeded From UniProt

complete

GO:0045449

regulation of transcription

PMID:12591879[18]

ECO:0000314

P

See Fig 4 and Table 2 supports the data of regulation of transcription

complete

GO:0009409

response to cold

PMID:21926233[19]

ECO:0000315

P

Figure 6 shows crp mutants show reduced cell growth compared to the WT at 15C.

complete
CACAO 2524

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Gosset, G et al. (2004) Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli. J. Bacteriol. 186 3516-24 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Limón, A et al. (1997) The aldA gene of Escherichia coli is under the control of at least three transcriptional regulators. Microbiology (Reading, Engl.) 143 ( Pt 6) 2085-95 PubMed GONUTS page
  3. ↑ 3.0 3.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Tzeng, SR & Kalodimos, CG (2013) Allosteric inhibition through suppression of transient conformational states. Nat. Chem. Biol. 9 462-5 PubMed GONUTS page
  5. ↑ Sharma, H et al. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc. Natl. Acad. Sci. U.S.A. 106 16604-9 PubMed GONUTS page
  6. ↑ Popovych, N et al. (2009) Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proc. Natl. Acad. Sci. U.S.A. 106 6927-32 PubMed GONUTS page
  7. ↑ Popovych, N et al. (2006) Dynamically driven protein allostery. Nat. Struct. Mol. Biol. 13 831-8 PubMed GONUTS page
  8. ↑ 8.0 8.1 8.2 Zheng, D et al. (2004) Identification of the CRP regulon using in vitro and in vivo transcriptional profiling. Nucleic Acids Res. 32 5874-93 PubMed GONUTS page
  9. ↑ Cirino, PC et al. (2006) Engineering Escherichia coli for xylitol production from glucose-xylose mixtures. Biotechnol. Bioeng. 95 1167-76 PubMed GONUTS page
  10. ↑ Williams, RM et al. (1996) Orientation of functional activating regions in the Escherichia coli CRP protein during transcription activation at class II promoters. Nucleic Acids Res. 24 1112-8 PubMed GONUTS page
  11. ↑ 11.0 11.1 Beatty, CM et al. (2003) Cyclic AMP receptor protein-dependent activation of the Escherichia coli acsP2 promoter by a synergistic class III mechanism. J. Bacteriol. 185 5148-57 PubMed GONUTS page
  12. ↑ 12.0 12.1 Ramseier, TM & Saier, MH Jr (1995) cAMP-cAMP receptor protein complex: five binding sites in the control region of the Escherichia coli mannitol operon. Microbiology (Reading, Engl.) 141 ( Pt 8) 1901-7 PubMed GONUTS page
  13. ↑ Wickstrum, JR et al. (2005) Cyclic AMP receptor protein and RhaR synergistically activate transcription from the L-rhamnose-responsive rhaSR promoter in Escherichia coli. J. Bacteriol. 187 6708-18 PubMed GONUTS page
  14. ↑ Wade, JT et al. (2001) A simple mechanism for co-dependence on two activators at an Escherichia coli promoter. EMBO J. 20 7160-7 PubMed GONUTS page
  15. ↑ Belyaeva, TA et al. (2000) Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein. Mol. Microbiol. 36 211-22 PubMed GONUTS page
  16. ↑ Shaw, DJ et al. (1983) Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. J. Mol. Biol. 166 241-7 PubMed GONUTS page
  17. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  18. ↑ Starcic, M et al. (2003) The cyclic AMP-cyclic AMP receptor protein complex regulates activity of the traJ promoter of the Escherichia coli conjugative plasmid pRK100. J. Bacteriol. 185 1616-23 PubMed GONUTS page
  19. ↑ Uppal, S et al. (2011) Cyclic AMP receptor protein regulates cspE, an early cold-inducible gene, in Escherichia coli. J. Bacteriol. 193 6142-51 PubMed GONUTS page
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=ECOLI:CRP&oldid=5953182"