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P0ACJ8 (CRP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catabolite gene activator
Alternative name(s):
cAMP receptor protein
cAMP regulatory protein
Gene names
Name:crp
Synonyms:cap, csm
Ordered Locus Names:b3357, JW5702
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA. Acts as a negative regulator of its own synthesis.

Subunit structure

Binds DNA as a dimer.

Sequence similarities

Contains 1 cyclic nucleotide-binding domain.

Contains 1 HTH crp-type DNA-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplLP0A7K21EBI-547513,EBI-543702

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210Catabolite gene activator
PRO_0000100144

Regions

Domain138 – 21073HTH crp-type
Nucleotide binding10 – 133124cAMP
DNA binding170 – 18920H-T-H motif

Sites

Binding site1291cAMP

Amino acid modifications

Modified residue1011N6-acetyllysine Ref.5

Experimental info

Mutagenesis631S → A: Enhanced cAMP-binding.
Mutagenesis831R → L: Loss of cAMP-binding.
Mutagenesis841S → A or K: No modification of cAMP-binding.
Mutagenesis1281T → A: No modification of cAMP-binding.
Mutagenesis1291S → A: Reduced DNA-binding; no modification of cAMP-binding.
Mutagenesis1811R → K: Suppresses DNA-binding.
Mutagenesis1811R → L: Suppresses DNA-binding.
Mutagenesis1861R → K: No modification of DNA-binding.
Mutagenesis1861R → L: Marginally reduced DNA-binding.
Sequence conflict291T → K in BAE77933. Ref.4

Secondary structure

..................................... 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ACJ8 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DCBC24FA46C61B3D

FASTA21023,640
        10         20         30         40         50         60 
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV LIKDEEGKEM 

        70         80         90        100        110        120 
ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY KKFRQLIQVN PDILMRLSAQ 

       130        140        150        160        170        180 
MARRLQVTSE KVGNLAFLDV TGRIAQTLLN LAKQPDAMTH PDGMQIKITR QEIGQIVGCS 

       190        200        210 
RETVGRILKM LEDQNLISAH GKTIVVYGTR 

« Hide

References

« Hide 'large scale' references
[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: 6280140] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 6280141] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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: 18723842] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[6]"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: 6286624] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[7]"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: 2828639] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[8]"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: 1653449] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH DNA.
[9]"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: 11124031] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[10]"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: 3333845] [Abstract]
Cited for: MUTAGENESIS.
[11]"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: 2845936] [Abstract]
Cited for: MUTAGENESIS.
[12]"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: 8394684] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01598 Genomic DNA. Translation: AAA23601.1.
U18997 Genomic DNA. Translation: AAA58154.1.
U00096 Genomic DNA. Translation: AAC76382.1.
AP009048 Genomic DNA. Translation: BAE77933.1.
PIRQRECC. A93416.
RefSeqNP_417816.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortalP0ACJ8.
SMRP0ACJ8. Positions 2-208.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29232N.
IntActP0ACJ8. 8 interactions.
MINTMINT-1249660.

2D gel databases

ECO2DBASEI021.4. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000004831; EBESCP00000004831; EBESCG00000003945.
EBESCT00000004832; EBESCP00000004832; EBESCG00000003945.
EBESCT00000004833; EBESCP00000004833; EBESCG00000003945.
EBESCT00000017422; EBESCP00000016713; EBESCG00000016478.
GeneID947867.
GenomeReviewsGene locus JW5702 in contig AP009048_GR.
Gene locus b3357 in contig U00096_GR.
KEGGecj:JW5702.
eco:b3357.
PATRIC32122148. VBIEscCol129921_3451.

Organism-specific databases

EchoBASEEB0162.
EcoGeneEG10164. crp.

Phylogenomic databases

eggNOGCOG0664.
GeneTreeEBGT00050000009957.
HOGENOMHBG648099.
OMARAKSACE.
PhylomeDBP0ACJ8.
ProtClustDBPRK11753.

Enzyme and pathway databases

BioCycEcoCyc:PD00257.

Gene expression databases

GenevestigatorP0ACJ8.

Family and domain databases

InterProIPR018490. 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_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK10914.
PfamPF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view]
PRINTSPR00034. HTHCRP.
SMARTSM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view]
SUPFAMSSF51206. cNMP_binding. 1 hit.
PROSITEPS00888. 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]
ProtoNetSearch...

Entry information

Entry nameCRP_ECOLI
AccessionPrimary (citable) accession number: P0ACJ8
Secondary accession number(s): P03020, Q2M723
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families