Entry Information
Protein Name Crp
Accession No P0ACJ8
Protein description Catabolite gene activator
pI/Mw (Da)
Theoretical Experimental
8.38/23640.43 8.56/25220
Protein function and expression This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of more than 200 genes.
Reference(s) Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)

2D gels information
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A D
pI/Mw: 8.56/25220

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
D
2-DE profile of E. coli proteins at the end of VEGF blank run fermentation.
Swiss-Prot Database Reference

Entry information
Entry Name CRP_ECOLI
Primary accession number P0ACJ8
Secondary accession numbers P03020 Q2M723 
Integrated into Swiss-Prot on 1986-07-21
Sequence was last modified on 1986-07-21 (Sequence version 1)
Annotations were last modified on 2006-06-27 (Entry version 9)
Name and origin of the protein
Protein name Catabolite gene activator
Synonyms Catabolite gene activator
cAMP receptor protein
cAMP-regulatory protein
Gene name Name : crp
OrderedLocusName : b3357
SynonymName : cap
SynonymName : csm
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA].PubMed=6280140[NCBI, ExPASy, EBI, Israel, Japan]
Aiba H. , Fujimoto S. , Ozaki N. ,
"Molecular cloning and nucleotide sequencing of the gene for E. coli cAMP receptor protein."
Nucleic Acids Res.10:1345-1361(1982) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12
PubMed=6280141[NCBI, ExPASy, EBI, Israel, Japan]
Cossart P. , Gicquel-Sanzey B. ,
"Cloning and sequence of the crp gene of Escherichia coli K 12."
Nucleic Acids Res.10:1363-1378(1982) 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
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. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[5] X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).PubMed=6286624[NCBI, ExPASy, EBI, Israel, Japan]
McKay D.B. , Weber I.T. , Steitz T.A. ,
"Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP."
J. Biol. Chem.257:9518-9524(1982) 
[6] X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).PubMed=2828639[NCBI, ExPASy, EBI, Israel, Japan]
Weber I.T. , Steitz T.A. ,
"Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5-A resolution."
J. Mol. Biol.198:311-326(1987) 
[7] X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH DNA.PubMed=1653449[NCBI, ExPASy, EBI, Israel, Japan]
Schultz S. , Shields G. , Steitz T.A. ,
"Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees."
Science253:1001-1007(1991) 
[8] X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).DOI=10.1006/jmbi.2000.4231;PubMed=11124031[NCBI, ExPASy, EBI, Israel, Japan]
Passner J.M. , Schultz S.C. , Steitz T.A. ,
"Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution."
J. Mol. Biol.304:847-859(2000) 
[9] MUTAGENESIS.PubMed=3333845[NCBI, ExPASy, EBI, Israel, Japan]
Gent M.E. , Gartner S. , Gronenborn A.M. , Sandulache R. , Clore G.M. ,
"Site-directed mutants of the cAMP receptor protein -- DNA binding of five mutant proteins."
Protein Eng.1:201-203(1987) 
[10] MUTAGENESIS.PubMed=2845936[NCBI, ExPASy, EBI, Israel, Japan]
Gronenborn A.M. , Sandulache R. , Clore G.M. ,
"Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli."
Biochem. J.253:801-807(1988) 
[11] REVIEW.DOI=10.1146/annurev.bi.62.070193.003533;PubMed=8394684[NCBI, ExPASy, EBI, Israel, Japan]
Kolb A. , Busby S. , Buc H. , Garges S. , Adhya S. ,
"Transcriptional regulation by cAMP and its receptor protein."
Annu. Rev. Biochem.62:749-795(1993) 
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 : Binds DNA as a dimer
  • SIMILARITY : Contains 1 cyclic nucleotide-binding domain
  • SIMILARITY : Contains 1 HTH crp-type DNA-binding domain
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL J01598;AAA23601.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U18997;AAA58154.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC76382.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAE77933.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR A93416;QRECC.
    3D structure databases
    PDB 1CGP;X-ray;A/B=2-206[ExPASy/RCSB/EBI].
    1G6N;X-ray;A/B=1-210[ExPASy/RCSB/EBI].
    1HW5;X-ray;A/B=1-210[ExPASy/RCSB/EBI].
    1I5Z;X-ray;A/B=2-210[ExPASy/RCSB/EBI].
    1I6X;X-ray;A/B=2-210[ExPASy/RCSB/EBI].
    1J59;X-ray;A/B=2-210[ExPASy/RCSB/EBI].
    1LB2;X-ray;A=2-210[ExPASy/RCSB/EBI].
    1O3Q;X-ray;A=9-208[ExPASy/RCSB/EBI].
    1O3R;X-ray;A=9-208[ExPASy/RCSB/EBI].
    1O3S;X-ray;A=9-208[ExPASy/RCSB/EBI].
    1O3T;X-ray;A/B=9-208[ExPASy/RCSB/EBI].
    1RUN;X-ray;A/B=2-210[ExPASy/RCSB/EBI].
    1RUO;X-ray;A/B=2-210[ExPASy/RCSB/EBI].
    2CGP;X-ray;A=1-210[ExPASy/RCSB/EBI].
    2GAP;Model;A/B=2-209[ExPASy/RCSB/EBI].
    Detailed list of linked structures
    ModBase P0ACJ8
    Protein-protein interaction databases
    DIP P0ACJ8
    Enzyme and pathway databases
    BioCyc EcoCyc:PD00257;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB0162;-.
    ECO2DBASE I021.4;6TH EDITION.
    EcoGene EG10164;crp.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR000595;cNMP_bd.
    IPR001808;HTH_Crp.
    IPR012318;HTH_CRP_2.
    IPR002197;HTH_Fis.
    IPR011991;Wing_hlx_DNA_bd.
    Graphical view of domain structure
    Pfam PF00027;cNMP_binding;1.
    PF00325;Crp;1.
    Pfam graphical view of domain structure
    PRINTS PR00034;HTHCRP.
    PR01590;HTHFIS.
    SMART SM00100;cNMP;1.
    SM00419;HTH_CRP;1.
    SMART graphical view of domain structure
    BLOCKS P0ACJ8
    PROSITE PS00888;CNMP_BINDING_1;1.
    PS00889;CNMP_BINDING_2;1.
    PS50042;CNMP_BINDING_3;1.
    PS00042;HTH_CRP_1;1.
    PS51063;HTH_CRP_2;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b3357.
    Other
    LinkHub P0ACJ8;-.
    ProtoNet P0ACJ8
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    3D-structure; Activator; cAMP; cAMP-binding; Complete proteome; DNA-binding; Nucleotide-binding; Transcription; Transcription regulation;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   210    210  Catabolite gene activator  PRO_0000100144
    DOMAIN  138   210     73  HTH crp-type  
    NP_BIND   10   133    124  cAMP  
    DNA_BIND  170   189     20  H-T-H motif  
    BINDING  129   129    cAMP  
    MUTAGEN   63    63    S -> A: Enhanced cAMP-binding  
    MUTAGEN   83    83    R -> L: Loss of cAMP-binding  
    MUTAGEN   84    84    S -> A: No modification of cAMP-binding  
    MUTAGEN  128   128    T -> A: No modification of cAMP-binding  
    MUTAGEN  129   129    S -> A: Reduced DNA-binding; no modification of cAMP-binding  
    MUTAGEN  181   181    R -> K: Suppresses DNA-binding  
    MUTAGEN  181   181    R -> L: Suppresses DNA-binding  
    MUTAGEN  186   186    R -> K: No modification of DNA-binding  
    MUTAGEN  186   186    R -> L: Marginally reduced DNA-binding  
    CONFLICT   29    29    T -> K: (in Ref. 4)  
    HELIX    9    16      8    
    TURN   17    18      2    
    STRAND   20    24      5    
    TURN   26    27      2    
    STRAND   29    31      3    
    TURN   33    34      2    
    STRAND   36    36      1    
    STRAND   39    45      7    
    STRAND   47    53      7    
    STRAND   59    66      8    
    TURN   67    68      2    
    STRAND   70    71      2    
    HELIX   74    76      3    
    STRAND   82    82      1    
    STRAND   86    89      4    
    STRAND   93    99      7    
    HELIX  100   109     10    
    TURN  111   111      1    
    HELIX  112   137     26    
    HELIX  140   151     12    
    TURN  152   152      1    
    TURN  155   156      2    
    STRAND  160   160      1    
    TURN  161   162      2    
    STRAND  163   167      5    
    HELIX  170   177      8    
    TURN  178   178      1    
    HELIX  181   193     13    
    TURN  194   195      2    
    STRAND  197   198      2    
    STRAND  202   205      4    
    Sequence information
    Length: 210AA [This is the length of the unprocessed precursor] Molecular weight: 23640Da [This is the MW of the unprocessed precursor] CRC64: DCBC24FA46C61B3D[This is a checksum on the sequence]
            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 
    P0ACJ8 in FASTA format