Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0ACJ8

- CRP_ECOLI

UniProt

P0ACJ8 - CRP_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

cAMP-activated global transcriptional regulator CRP

Gene

crp

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-3') to directly regulate the transcription of about 300 genes in about 200 operons and indirectly regulate the expression of about half the genome. There are 3 classes of CRP promoters; class I promoters have a single CRP-binding site upstream of the RNA polymerase (RNAP)-binding site, whereas in class II promoters the single CRP- and RNAP-binding site overlap, CRP making multiple contacts with RNAP. Class III promoters require multiple activator molecules, including at least one CRP dimer. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA (about 87 degrees), bringing upstream promoter elements into contact with RNAP. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. High levels of active CRP are detrimental to growth (PubMed:16260780). Plays a major role in carbon catabolite repression (CCR). CCR involves cAMP, adenylate cyclase (cyaA), CRP and the EIIA-Glc component of the PTS (crr). In the presence of glucose EIIA-Glc is dephosphorylated, and does not activate adenylate cyclase, leading to reduced cAMP and thus decreased CRP activity. Also plays a role in many other processes (see PubMed:22573269).10 Publications

Enzyme regulationi

In the apo-form the DNA-binding helices form a rigid body in which their DNA recognitions helices are buried. cAMP binding causes a coil-to helix transition, stabilizing the active DNA binding conformation by reorienting and elongating these helices, which precludes a return to the inactive state.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei97 – 971Activating region 2 (AR2); probably contacts the N-terminus of RpoA
Sitei102 – 1021Activating region 2 (AR2); probably contacts the N-terminus of RpoA
Binding sitei129 – 1291cAMP6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi57 – 637cAMP 16 Publications
Nucleotide bindingi72 – 743cAMP 16 Publications
Nucleotide bindingi83 – 842cAMP 16 Publications
Nucleotide bindingi128 – 1292cAMP 16 Publications
Nucleotide bindingi136 – 1372cAMP 26 Publications
Nucleotide bindingi171 – 18111cAMP 26 PublicationsAdd
BLAST
DNA bindingi180 – 1867H-T-H motifPROSITE-ProRule annotation

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. carbon catabolite repression of transcription Source: EcoCyc
  2. negative regulation of transcription, DNA-templated Source: EcoliWiki
  3. positive regulation of transcription, DNA-templated Source: EcoliWiki
  4. transcription, DNA-templated Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

cAMP, cAMP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00257.
ECOL316407:JW5702-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-activated global transcriptional regulator CRP
Alternative name(s):
Catabolite activator protein
Short name:
CAP
Catabolite gene activator
cAMP receptor protein
Short name:
CRP
cAMP regulatory protein
Gene namesi
Name:crp
Synonyms:cap, csm
Ordered Locus Names:b3357, JW5702
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10164. crp.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Not essential (on rich medium), greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201H → A, L or Y: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication
Mutagenesisi22 – 221H → A or L: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication
Mutagenesisi53 – 531K → N: Increased activation at class II promoters, increased interaction with RNAP. 1 Publication
Mutagenesisi54 – 563DEE → AAA: 80% reduction in activation of class II promoters; 95% loss when associated with A-59. 1 Publication
Mutagenesisi59 – 591E → A: 45% reduction in activation of class II promoters; 95% loss when associated with AAA-54-56. 2 Publications
Mutagenesisi59 – 591E → G or K: Reduction in activation of class II promoters. 2 Publications
Mutagenesisi63 – 631S → A: Enhanced cAMP-binding, enhanced transcription. 1 Publication
Mutagenesisi83 – 831R → L: Loss of cAMP-binding. 1 Publication
Mutagenesisi84 – 841S → A or K: No modification of cAMP-binding. 1 Publication
Mutagenesisi97 – 971E → A: Increased transcription activation at class II promoters, binds DNA. 1 Publication
Mutagenesisi102 – 1021K → E: Disrupts AR2. No activation of class II promoters, decreased interaction with RNAP, binds DNA. 2 Publications
Mutagenesisi128 – 1292TS → LI: Constitutively active at class I and II promoters in the absence of cAMP, binds DNA almost as well in the absence as in the presence of cAMP. Binds cAMP normally. 2 Publications
Mutagenesisi128 – 1281T → A: No modification of cAMP-binding. 1 Publication
Mutagenesisi129 – 1291S → A: Reduced DNA-binding; no modification of cAMP-binding. 2 Publications
Mutagenesisi139 – 1391D → L: Some stabilization of an inactive (apo-) form. Decreased affinity for DNA, normal subunit association. 3 Publications
Mutagenesisi157 – 1571A → D or P: Decreased transcription activation (6-29%), binds DNA. 2 Publications
Mutagenesisi159 – 1591T → A, I, N, S or V: Decreased transcription activation (15-87%) at class I and II promoters, binds DNA. 3 Publications
Mutagenesisi160 – 1601H → A, K, L, N, P, Q, R or Y: Disrupts AR1. Decreased transcription activation (3-45%) at class I and II promoters, binds DNA. 4 Publications
Mutagenesisi163 – 1631G → A, C, D, R, S or V: Decreased transcription activation (2-62%) at class I and II promoters, binds DNA. 3 Publications
Mutagenesisi181 – 1811R → K: Suppresses DNA-binding. 1 Publication
Mutagenesisi181 – 1811R → L: Suppresses DNA-binding. 1 Publication
Mutagenesisi186 – 1861R → K: No modification of DNA-binding. 1 Publication
Mutagenesisi186 – 1861R → L: Marginally reduced DNA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 210209cAMP-activated global transcriptional regulator CRPPRO_0000100144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0ACJ8.
PRIDEiP0ACJ8.

Expressioni

Inductioni

Constitutively expressed, levels decrease in stationary phase; more strongly induced in an rnlA deletion mutant, levels remain high even in stationary phase (at protein level). Both positively (PubMed:1328816) and negatively autoregulated (PubMed:6297782).3 Publications

Gene expression databases

GenevestigatoriP0ACJ8.

Interactioni

Subunit structurei

Homodimer, which upon binding cAMP is able to bind DNA. AR1 of the upstream subunit binds to the C-terminus of RNAP subunit RpoA, AR2 of the downstream subunit binds to the N-terminus of RpoA while AR3 binds to sigma-70 (RpoD).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
nusGP0AFG02EBI-547513,EBI-369628
priCP238622EBI-547513,EBI-1117383
yacLP0A8E53EBI-547513,EBI-554965

Protein-protein interaction databases

DIPiDIP-29232N.
IntActiP0ACJ8. 39 interactions.
MINTiMINT-1249660.
STRINGi511145.b3357.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 178
Beta strandi19 – 246
Beta strandi29 – 313
Beta strandi33 – 364
Beta strandi39 – 457
Beta strandi47 – 537
Beta strandi55 – 573
Beta strandi59 – 668
Beta strandi70 – 723
Turni74 – 774
Beta strandi78 – 803
Beta strandi85 – 917
Beta strandi93 – 997
Helixi100 – 10910
Helixi112 – 13726
Helixi140 – 15213
Beta strandi154 – 1563
Beta strandi158 – 1603
Beta strandi163 – 1675
Helixi170 – 1778
Helixi181 – 19313
Beta strandi196 – 2005
Beta strandi203 – 2075

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CGPX-ray3.00A/B2-206[»]
1G6NX-ray2.10A/B1-210[»]
1HW5X-ray1.82A/B1-210[»]
1I5ZX-ray1.90A/B2-210[»]
1I6XX-ray2.20A/B2-210[»]
1J59X-ray2.50A/B2-210[»]
1LB2X-ray3.10A2-210[»]
1O3QX-ray3.00A9-208[»]
1O3RX-ray3.00A9-208[»]
1O3SX-ray3.00A9-208[»]
1O3TX-ray2.80A/B9-208[»]
1RUNX-ray2.70A/B2-210[»]
1RUOX-ray2.70A/B2-210[»]
1ZRCX-ray2.80A/B2-210[»]
1ZRDX-ray2.80A/B2-210[»]
1ZREX-ray2.80A/B2-210[»]
1ZRFX-ray2.10A/B2-210[»]
2CGPX-ray2.20A1-210[»]
2GAPmodel-A/B2-209[»]
2GZWX-ray2.21A/B/C/D2-210[»]
2WC2NMR-A/B2-210[»]
3FWEX-ray2.30A/B1-210[»]
3HIFX-ray3.59A/B/C/D/E/F1-210[»]
3IYDelectron microscopy-G/H2-210[»]
3KCCX-ray1.66A/B1-210[»]
3N4MX-ray2.99A2-210[»]
3QOPX-ray1.96A/B1-210[»]
3RDIX-ray2.95A/B1-210[»]
3ROUX-ray2.10A/B1-210[»]
3RPQX-ray2.61A/B1-210[»]
3RYPX-ray1.60A/B1-210[»]
3RYRX-ray2.70A/B1-210[»]
4BH9NMR-A2-210[»]
4BHPNMR-A2-210[»]
4FT8X-ray1.97A/B2-210[»]
4HZFX-ray1.48A/B1-210[»]
4I01X-ray2.30A/B1-210[»]
4I02X-ray1.75A/B/C/D/E/F1-210[»]
4I09X-ray2.05A/B1-210[»]
4I0AX-ray2.20A/B1-210[»]
4I0BX-ray1.50A/B1-210[»]
ProteinModelPortaliP0ACJ8.
SMRiP0ACJ8. Positions 9-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACJ8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 21073HTH crp-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 223Activating region 2 (AR2); probably contacts the N-terminus of RpoA
Regioni53 – 597Activating region 3 (AR3); probably contacts sigma-70 (RpoD)
Regioni154 – 16310Activating region 1 (AR1); probably contacts the C-terminus of RpoA

Domaini

The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound.2 Publications

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 HTH crp-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0664.
HOGENOMiHOG000250565.
InParanoidiP0ACJ8.
KOiK10914.
OMAiSETHPEF.
OrthoDBiEOG69GZGV.
PhylomeDBiP0ACJ8.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR012318. HTH_CRP_2.
IPR014710. RmlC-like_jellyroll.
IPR001808. Tscrpt_reg_HTH_Crp.
IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view]
PRINTSiPR00034. HTHCRP.
SMARTiSM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
PS00042. HTH_CRP_1. 1 hit.
PS51063. HTH_CRP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ACJ8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV
60 70 80 90 100
LIKDEEGKEM ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY
110 120 130 140 150
KKFRQLIQVN PDILMRLSAQ MARRLQVTSE KVGNLAFLDV TGRIAQTLLN
160 170 180 190 200
LAKQPDAMTH PDGMQIKITR QEIGQIVGCS RETVGRILKM LEDQNLISAH
210
GKTIVVYGTR
Length:210
Mass (Da):23,640
Last modified:July 21, 1986 - v1
Checksum:iDCBC24FA46C61B3D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291T → K in BAE77933. (PubMed:16738553)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01598 Genomic DNA. Translation: AAA23601.1.
U18997 Genomic DNA. Translation: AAA58154.1.
U00096 Genomic DNA. Translation: AAC76382.1.
AP009048 Genomic DNA. Translation: BAE77933.1.
PIRiA93416. QRECC.
RefSeqiNP_417816.1. NC_000913.3.
YP_492074.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76382; AAC76382; b3357.
BAE77933; BAE77933; BAE77933.
GeneIDi12933934.
947867.
KEGGiecj:Y75_p3818.
eco:b3357.
PATRICi32122148. VBIEscCol129921_3451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01598 Genomic DNA. Translation: AAA23601.1 .
U18997 Genomic DNA. Translation: AAA58154.1 .
U00096 Genomic DNA. Translation: AAC76382.1 .
AP009048 Genomic DNA. Translation: BAE77933.1 .
PIRi A93416. QRECC.
RefSeqi NP_417816.1. NC_000913.3.
YP_492074.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CGP X-ray 3.00 A/B 2-206 [» ]
1G6N X-ray 2.10 A/B 1-210 [» ]
1HW5 X-ray 1.82 A/B 1-210 [» ]
1I5Z X-ray 1.90 A/B 2-210 [» ]
1I6X X-ray 2.20 A/B 2-210 [» ]
1J59 X-ray 2.50 A/B 2-210 [» ]
1LB2 X-ray 3.10 A 2-210 [» ]
1O3Q X-ray 3.00 A 9-208 [» ]
1O3R X-ray 3.00 A 9-208 [» ]
1O3S X-ray 3.00 A 9-208 [» ]
1O3T X-ray 2.80 A/B 9-208 [» ]
1RUN X-ray 2.70 A/B 2-210 [» ]
1RUO X-ray 2.70 A/B 2-210 [» ]
1ZRC X-ray 2.80 A/B 2-210 [» ]
1ZRD X-ray 2.80 A/B 2-210 [» ]
1ZRE X-ray 2.80 A/B 2-210 [» ]
1ZRF X-ray 2.10 A/B 2-210 [» ]
2CGP X-ray 2.20 A 1-210 [» ]
2GAP model - A/B 2-209 [» ]
2GZW X-ray 2.21 A/B/C/D 2-210 [» ]
2WC2 NMR - A/B 2-210 [» ]
3FWE X-ray 2.30 A/B 1-210 [» ]
3HIF X-ray 3.59 A/B/C/D/E/F 1-210 [» ]
3IYD electron microscopy - G/H 2-210 [» ]
3KCC X-ray 1.66 A/B 1-210 [» ]
3N4M X-ray 2.99 A 2-210 [» ]
3QOP X-ray 1.96 A/B 1-210 [» ]
3RDI X-ray 2.95 A/B 1-210 [» ]
3ROU X-ray 2.10 A/B 1-210 [» ]
3RPQ X-ray 2.61 A/B 1-210 [» ]
3RYP X-ray 1.60 A/B 1-210 [» ]
3RYR X-ray 2.70 A/B 1-210 [» ]
4BH9 NMR - A 2-210 [» ]
4BHP NMR - A 2-210 [» ]
4FT8 X-ray 1.97 A/B 2-210 [» ]
4HZF X-ray 1.48 A/B 1-210 [» ]
4I01 X-ray 2.30 A/B 1-210 [» ]
4I02 X-ray 1.75 A/B/C/D/E/F 1-210 [» ]
4I09 X-ray 2.05 A/B 1-210 [» ]
4I0A X-ray 2.20 A/B 1-210 [» ]
4I0B X-ray 1.50 A/B 1-210 [» ]
ProteinModelPortali P0ACJ8.
SMRi P0ACJ8. Positions 9-208.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29232N.
IntActi P0ACJ8. 39 interactions.
MINTi MINT-1249660.
STRINGi 511145.b3357.

Proteomic databases

PaxDbi P0ACJ8.
PRIDEi P0ACJ8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76382 ; AAC76382 ; b3357 .
BAE77933 ; BAE77933 ; BAE77933 .
GeneIDi 12933934.
947867.
KEGGi ecj:Y75_p3818.
eco:b3357.
PATRICi 32122148. VBIEscCol129921_3451.

Organism-specific databases

EchoBASEi EB0162.
EcoGenei EG10164. crp.

Phylogenomic databases

eggNOGi COG0664.
HOGENOMi HOG000250565.
InParanoidi P0ACJ8.
KOi K10914.
OMAi SETHPEF.
OrthoDBi EOG69GZGV.
PhylomeDBi P0ACJ8.

Enzyme and pathway databases

BioCyci EcoCyc:PD00257.
ECOL316407:JW5702-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ACJ8.
PROi P0ACJ8.

Gene expression databases

Genevestigatori P0ACJ8.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProi IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR012318. HTH_CRP_2.
IPR014710. RmlC-like_jellyroll.
IPR001808. Tscrpt_reg_HTH_Crp.
IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view ]
PRINTSi PR00034. HTHCRP.
SMARTi SM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view ]
SUPFAMi SSF51206. SSF51206. 1 hit.
PROSITEi PS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
PS00042. HTH_CRP_1. 1 hit.
PS51063. HTH_CRP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequencing of the gene for E. coli cAMP receptor protein."
    Aiba H., Fujimoto S., Ozaki N.
    Nucleic Acids Res. 10:1345-1361(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CAMP-BINDING.
    Strain: K12.
  2. "Cloning and sequence of the crp gene of Escherichia coli K 12."
    Cossart P., Gicquel-Sanzey B.
    Nucleic Acids Res. 10:1363-1378(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "A role of RnlA in the RNase LS activity from Escherichia coli."
    Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
    Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10.
    Strain: K12.
  6. "Deletion of the Escherichia coli crp gene."
    Sabourin D., Beckwith J.
    J. Bacteriol. 122:338-340(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own gene."
    Aiba H.
    Cell 32:141-149(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, NEGATIVE AUTOREGULATION, DNA-BINDING.
  8. "Transcription of the Escherichia coli adenylate cyclase gene is negatively regulated by cAMP-cAMP receptor protein."
    Aiba H.
    J. Biol. Chem. 260:3063-3070(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, AUTOREGULATION, DNA-BINDING.
  9. "Site-directed mutants of the cAMP receptor protein -- DNA binding of five mutant proteins."
    Gent M.E., Gartner S., Gronenborn A.M., Sandulache R., Clore G.M.
    Protein Eng. 1:201-203(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, MUTAGENESIS OF SER-129; ARG-181 AND ARG-186.
  10. "Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli."
    Gronenborn A.M., Sandulache R., Clore G.M.
    Biochem. J. 253:801-807(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CAMP-BINDING, MUTAGENESIS OF SER-63; ARG-83; SER-84; THR-128 AND SER-129.
  11. "Binding of the cyclic AMP receptor protein of Escherichia coli to RNA polymerase."
    Pinkney M., Hoggett J.G.
    Biochem. J. 250:897-902(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CAMP-BINDING, INTERACTION WITH RNA POLYMERASE, SUBUNIT.
    Strain: MRE-600.
  12. "Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP."
    Igarashi K., Ishihama A.
    Cell 65:1015-1022(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ACTIVTOR, FUNCTION AS A REPRESSOR, PROBABLE INTERACTION WITH RPOA, SUBUNIT.
  13. "A new aspect of transcriptional control of the Escherichia coli crp gene: positive autoregulation."
    Hanamura A., Aiba H.
    Mol. Microbiol. 6:2489-2497(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTON, POSITIVE AUTOREGULATION.
  14. "Pivotal role of amino acid at position 138 in the allosteric hinge reorientation of cAMP receptor protein."
    Ryu S., Kim J., Adhya S., Garges S.
    Proc. Natl. Acad. Sci. U.S.A. 90:75-79(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-139.
  15. "Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants of CAP specifically defective in transcription activation."
    Zhou Y., Zhang X., Ebright R.H.
    Proc. Natl. Acad. Sci. U.S.A. 90:6081-6085(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 1 (AR1), DNA-BINDING, MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163.
  16. "Characterization of the activating region of Escherichia coli catabolite gene activator protein (CAP). I. Saturation and alanine-scanning mutagenesis."
    Niu W., Zhou Y., Dong Q., Ebright Y.W., Ebright R.H.
    J. Mol. Biol. 243:595-602(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 1 (AR1), DNA-BINDING, MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163.
    Strain: K12.
  17. "Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase."
    Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.
    Cell 87:1123-1134(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 2 (AR2), INTERACTION WITH RPOA, DNA-BINDING, DNA-BENDING, MUTAGENESIS OF HIS-20; HIS-22; LYS-53; GLU-97; LYS-102; THR-159; HIS-160 AND GLY-163.
  18. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  19. "Transcription activation by the Escherichia coli cyclic AMP receptor protein: determinants within activating region 3."
    Rhodius V.A., Busby S.J.
    J. Mol. Biol. 299:295-310(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 3 (AR3), MUTAGENESIS OF 54-ASP--GLU-56 AND GLU-59.
  20. "Interactions between activating region 3 of the Escherichia coli cyclic AMP receptor protein and region 4 of the RNA polymerase sigma(70) subunit: application of suppression genetics."
    Rhodius V.A., Busby S.J.
    J. Mol. Biol. 299:311-324(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 3 (AR3), PROBABLE INTERACTION WITH SIGMA-70 (RPOD), MUTAGENESIS OF GLU-59.
  21. "Role of residue 138 in the interdomain hinge region in transmitting allosteric signals for DNA binding in Escherichia coli cAMP receptor protein."
    Yu S., Lee J.C.
    Biochemistry 43:4662-4669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-139.
  22. "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling."
    Zheng D., Constantinidou C., Hobman J.L., Minchin S.D.
    Nucleic Acids Res. 32:5874-5893(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REGULON, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-102 AND HIS-160.
    Strain: K12 / MG1655 / ATCC 47076.
  23. "Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome."
    Grainger D.C., Hurd D., Harrison M., Holdstock J., Busby S.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:17693-17698(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REGULON.
    Strain: K12 / MG1655 / ATCC 47076.
  24. "Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein."
    Youn H., Kerby R.L., Conrad M., Roberts G.P.
    J. Biol. Chem. 281:1119-1127(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 128-THR-SER-129.
  25. "Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia coli."
    Iwamoto A., Lemire S., Yonesaki T.
    Mol. Microbiol. 70:1570-1578(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DISRUPTION PHENOTYPE.
    Strain: K12.
  26. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  27. "Transcriptional regulation by cAMP and its receptor protein."
    Kolb A., Busby S., Buc H., Garges S., Adhya S.
    Annu. Rev. Biochem. 62:749-795(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  28. "Transcription activation by catabolite activator protein (CAP)."
    Busby S., Ebright R.H.
    J. Mol. Biol. 293:199-213(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  29. "Structural overview on the allosteric activation of cyclic AMP receptor protein."
    Won H.S., Lee Y.S., Lee S.H., Lee B.J.
    Biochim. Biophys. Acta 1794:1299-1308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  30. "Current knowledge of the Escherichia coli phosphoenolpyruvate-carbohydrate phosphotransferase system: peculiarities of regulation and impact on growth and product formation."
    Escalante A., Salinas Cervantes A., Gosset G., Bolivar F.
    Appl. Microbiol. Biotechnol. 94:1483-1494(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN CARBON CATABOLITE REPRESSION AND OTHER PROCESSES.
  31. "Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP."
    McKay D.B., Weber I.T., Steitz T.A.
    J. Biol. Chem. 257:9518-9524(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT, DOMAIN.
  32. "Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5-A resolution."
    Weber I.T., Steitz T.A.
    J. Mol. Biol. 198:311-326(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT, DOMAIN.
  33. "Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees."
    Schultz S., Shields G., Steitz T.A.
    Science 253:1001-1007(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-206 IN COMPLEX WITH CAMP AND DNA, SUBUNIT, DNA-BINDING, DNA-BENDING.
  34. "Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface."
    Parkinson G., Wilson C., Gunasekera A., Ebright Y.W., Ebright R.H., Berman H.M.
    J. Mol. Biol. 260:395-408(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP AND DNA, SUBUNIT, DNA-BINDING, DNA-BENDING.
  35. "The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer."
    Passner J.M., Steitz T.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:2843-2847(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH 2 CAMP PER MONOMER AND DNA, SUBUNIT, DNA-BINDING.
  36. "Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution."
    Passner J.M., Schultz S.C., Steitz T.A.
    J. Mol. Biol. 304:847-859(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT.
  37. "Structural basis of transcription activation: the CAP-alpha CTD-DNA complex."
    Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E., Ebright Y.W., Berman H.M., Ebright R.H.
    Science 297:1562-1566(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP; DNA AND RNAP, INTERACTION WITH RPOA, DNA-BINDING, SUBUNIT.
  38. "Structural basis for cAMP-mediated allosteric control of the catabolite activator protein."
    Popovych N., Tzeng S.R., Tonelli M., Ebright R.H., Kalodimos C.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:6927-6932(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-210 OF APO-CRP, ENZYME REGULATION, SUBUNIT.
  39. "Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding."
    Sharma H., Yu S., Kong J., Wang J., Steitz T.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:16604-16609(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APO-CRP, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF ASP-139.
  40. "Three-dimensional EM structure of an intact activator-dependent transcription initiation complex."
    Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., Ebright R.H., Lawson C.L.
    Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) OF 2-210 IN COMPLEX WITH RPOA; RPOB; RPOC; RPOD; RPOZ AND DNA, INTERACTION WITH ROPA, DNA-BINDING, SUBUNIT.
  41. "Crystal structure of activated CRP protein from E.coli."
    Kumarevel T.S., Tanaka T., Shinkai A., Yokoyama S.
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-210 IN COMPLEX WITH 2 CAMP PER MONOMER, SUBUNIT.
  42. "Allosteric inhibition through suppression of transient conformational states."
    Tzeng S.R., Kalodimos C.G.
    Nat. Chem. Biol. 9:462-465(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-210 OF APO-CRP, MUTAGENESIS OF 128-THR-SER-129.

Entry informationi

Entry nameiCRP_ECOLI
AccessioniPrimary (citable) accession number: P0ACJ8
Secondary accession number(s): P03020, Q2M723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds 2 cAMP; cAMP 1 is in the anti conformation, while cAMP 2 is in the syn conformation.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3