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P0ACJ8 (CRP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 84. 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:
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 names
Name:crp
Synonyms:cap, csm
Ordered Locus Names:b3357, JW5702
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (Ref.24). 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 Ref.30). Ref.8 Ref.12 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24

Enzyme regulation

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. Ref.38 Ref.39

Subunit structure

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). Ref.11 Ref.12 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41

Induction

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 (Ref.13) and negatively autoregulated (Ref.7). Ref.7 Ref.8 Ref.13 Ref.25 Ref.38 Ref.39

Domain

The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound. Ref.31 Ref.32

Disruption phenotype

Not essential (on rich medium), greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant. Ref.6 Ref.22 Ref.25

Miscellaneous

Binds 2 cAMP; cAMP 1 is in the anti conformation, while cAMP 2 is in the syn conformation (Ref.35).

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

Initiator methionine11Removed Ref.5
Chain2 – 210209cAMP-activated global transcriptional regulator CRP
PRO_0000100144

Regions

Domain138 – 21073HTH crp-type
Nucleotide binding57 – 637cAMP 1
Nucleotide binding72 – 743cAMP 1
Nucleotide binding83 – 842cAMP 1
Nucleotide binding128 – 1292cAMP 1
Nucleotide binding136 – 1372cAMP 2
Nucleotide binding171 – 18111cAMP 2
DNA binding180 – 1867H-T-H motif Ref.7 Ref.8 Ref.9 Ref.15 Ref.16 Ref.17 Ref.33 Ref.34 Ref.35 Ref.37 Ref.40
Region20 – 223Activating region 2 (AR2); probably contacts the N-terminus of RpoA
Region53 – 597Activating region 3 (AR3); probably contacts sigma-70 (RpoD)
Region154 – 16310Activating region 1 (AR1); probably contacts the C-terminus of RpoA

Sites

Binding site1291cAMP
Site971Activating region 2 (AR2); probably contacts the N-terminus of RpoA
Site1021Activating region 2 (AR2); probably contacts the N-terminus of RpoA

Amino acid modifications

Modified residue1011N6-acetyllysine Ref.26

Experimental info

Mutagenesis201H → A, L or Y: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. Ref.17 Ref.24 Ref.42
Mutagenesis221H → A or L: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. Ref.17 Ref.24 Ref.42
Mutagenesis531K → N: Increased activation at class II promoters, increased interaction with RNAP. Ref.17 Ref.24 Ref.42
Mutagenesis54 – 563DEE → AAA: 80% reduction in activation of class II promoters; 95% loss when associated with A-59. Ref.19 Ref.24 Ref.42
Mutagenesis591E → A: 45% reduction in activation of class II promoters; 95% loss when associated with AAA-54-56. Ref.19 Ref.20 Ref.24 Ref.42
Mutagenesis591E → G or K: Reduction in activation of class II promoters. Ref.19 Ref.20 Ref.24 Ref.42
Mutagenesis631S → A: Enhanced cAMP-binding, enhanced transcription. Ref.10 Ref.24 Ref.42
Mutagenesis831R → L: Loss of cAMP-binding. Ref.10 Ref.24 Ref.42
Mutagenesis841S → A or K: No modification of cAMP-binding. Ref.10 Ref.24 Ref.42
Mutagenesis971E → A: Increased transcription activation at class II promoters, binds DNA. Ref.17 Ref.24 Ref.42
Mutagenesis1021K → E: Disrupts AR2. No activation of class II promoters, decreased interaction with RNAP, binds DNA. Ref.17 Ref.22 Ref.24 Ref.42
Mutagenesis128 – 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. Ref.9 Ref.10 Ref.24 Ref.42
Mutagenesis1281T → A: No modification of cAMP-binding. Ref.10 Ref.24 Ref.42
Mutagenesis1291S → A: Reduced DNA-binding; no modification of cAMP-binding. Ref.9 Ref.10 Ref.24 Ref.42
Mutagenesis1391D → L: Some stabilization of an inactive (apo-) form. Decreased affinity for DNA, normal subunit association. Ref.14 Ref.21 Ref.24 Ref.39 Ref.42
Mutagenesis1571A → D or P: Decreased transcription activation (6-29%), binds DNA. Ref.15 Ref.16 Ref.24 Ref.42
Mutagenesis1591T → A, I, N, S or V: Decreased transcription activation (15-87%) at class I and II promoters, binds DNA. Ref.15 Ref.16 Ref.17 Ref.24 Ref.42
Mutagenesis1601H → A, K, L, N, P, Q, R or Y: Disrupts AR1. Decreased transcription activation (3-45%) at class I and II promoters, binds DNA. Ref.15 Ref.16 Ref.17 Ref.22 Ref.24 Ref.42
Mutagenesis1631G → A, C, D, R, S or V: Decreased transcription activation (2-62%) at class I and II promoters, binds DNA. Ref.15 Ref.16 Ref.17 Ref.24 Ref.42
Mutagenesis1811R → K: Suppresses DNA-binding. Ref.9 Ref.24 Ref.42
Mutagenesis1811R → L: Suppresses DNA-binding. Ref.9 Ref.24 Ref.42
Mutagenesis1861R → K: No modification of DNA-binding. Ref.9 Ref.24 Ref.42
Mutagenesis1861R → L: Marginally reduced DNA-binding. Ref.9 Ref.24 Ref.42
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] [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]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [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, 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.
+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_000913.3.
YP_492074.1. NC_007779.1.

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[»]
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[»]
ProteinModelPortalP0ACJ8.
SMRP0ACJ8. Positions 9-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29232N.
IntActP0ACJ8. 9 interactions.
MINTMINT-1249660.
STRING511145.b3357.

Proteomic databases

PaxDbP0ACJ8.
PRIDEP0ACJ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76382; AAC76382; b3357.
BAE77933; BAE77933; BAE77933.
GeneID12933934.
947867.
KEGGecj:Y75_p3818.
eco:b3357.
PATRIC32122148. VBIEscCol129921_3451.

Organism-specific databases

EchoBASEEB0162.
EcoGeneEG10164. crp.

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000250565.
KOK10914.
OMADQLYFIV.
OrthoDBEOG69GZGV.
ProtClustDBPRK11753.

Enzyme and pathway databases

BioCycEcoCyc:PD00257.
ECOL316407:JW5702-MONOMER.

Gene expression databases

GenevestigatorP0ACJ8.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
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_DNA-bd_dom.
[Graphical view]
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. SSF51206. 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...

Other

EvolutionaryTraceP0ACJ8.
PROP0ACJ8.

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: March 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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