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cAMP-activated global transcriptional regulator CRP (Catabolite activator protein) (CAP) (Catabolite gene activator) (cAMP receptor protein) (CRP) (cAMP regulatory protein)

 CRP_ECOLI               Reviewed;         210 AA.
P0ACJ8; P03020; Q2M723;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 112.
RecName: Full=cAMP-activated global transcriptional regulator CRP;
AltName: Full=Catabolite activator protein;
Short=CAP;
AltName: Full=Catabolite gene activator;
AltName: Full=cAMP receptor protein;
Short=CRP;
AltName: Full=cAMP regulatory protein;
Name=crp; Synonyms=cap, csm; OrderedLocusNames=b3357, JW5702;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CAMP-BINDING.
STRAIN=K12;
PubMed=6280140; DOI=10.1093/nar/10.4.1345;
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; DOI=10.1093/nar/10.4.1363;
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;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; 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]
PROTEIN SEQUENCE OF 2-10.
STRAIN=K12;
PubMed=17895580; DOI=10.1266/ggs.82.291;
Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
"A role of RnlA in the RNase LS activity from Escherichia coli.";
Genes Genet. Syst. 82:291-299(2007).
[6]
DISRUPTION PHENOTYPE.
PubMed=164435;
Sabourin D., Beckwith J.;
"Deletion of the Escherichia coli crp gene.";
J. Bacteriol. 122:338-340(1975).
[7]
INDUCTION, NEGATIVE AUTOREGULATION, AND DNA-BINDING.
PubMed=6297782; DOI=10.1016/0092-8674(83)90504-4;
Aiba H.;
"Autoregulation of the Escherichia coli crp gene: CRP is a
transcriptional repressor for its own gene.";
Cell 32:141-149(1983).
[8]
FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, AUTOREGULATION, AND
DNA-BINDING.
PubMed=2982847;
Aiba H.;
"Transcription of the Escherichia coli adenylate cyclase gene is
negatively regulated by cAMP-cAMP receptor protein.";
J. Biol. Chem. 260:3063-3070(1985).
[9]
DNA-BINDING, AND MUTAGENESIS OF SER-129; ARG-181 AND ARG-186.
PubMed=3333845; DOI=10.1093/protein/1.3.201;
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]
CAMP-BINDING, AND MUTAGENESIS OF SER-63; ARG-83; SER-84; THR-128 AND
SER-129.
PubMed=2845936; DOI=10.1042/bj2530801;
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]
CAMP-BINDING, INTERACTION WITH RNA POLYMERASE, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=2839152; DOI=10.1042/bj2500897;
Pinkney M., Hoggett J.G.;
"Binding of the cyclic AMP receptor protein of Escherichia coli to RNA
polymerase.";
Biochem. J. 250:897-902(1988).
[12]
FUNCTION AS AN ACTIVATOR, FUNCTION AS A REPRESSOR, PROBABLE
INTERACTION WITH RPOA, AND SUBUNIT.
PubMed=1646077; DOI=10.1016/0092-8674(91)90553-B;
Igarashi K., Ishihama A.;
"Bipartite functional map of the E. coli RNA polymerase alpha subunit:
involvement of the C-terminal region in transcription activation by
cAMP-CRP.";
Cell 65:1015-1022(1991).
[13]
INDUCTION, AND POSITIVE AUTOREGULATION.
PubMed=1328816;
Hanamura A., Aiba H.;
"A new aspect of transcriptional control of the Escherichia coli crp
gene: positive autoregulation.";
Mol. Microbiol. 6:2489-2497(1992).
[14]
MUTAGENESIS OF ASP-139.
PubMed=8380500; DOI=10.1073/pnas.90.1.75;
Ryu S., Kim J., Adhya S., Garges S.;
"Pivotal role of amino acid at position 138 in the allosteric hinge
reorientation of cAMP receptor protein.";
Proc. Natl. Acad. Sci. U.S.A. 90:75-79(1993).
[15]
FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 1 (AR1), DNA-BINDING,
AND MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163.
PubMed=8392187; DOI=10.1073/pnas.90.13.6081;
Zhou Y., Zhang X., Ebright R.H.;
"Identification of the activating region of catabolite gene activator
protein (CAP): isolation and characterization of mutants of CAP
specifically defective in transcription activation.";
Proc. Natl. Acad. Sci. U.S.A. 90:6081-6085(1993).
[16]
FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 1 (AR1), DNA-BINDING,
AND MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163.
STRAIN=K12;
PubMed=7966284; DOI=10.1016/0022-2836(94)90034-5;
Niu W., Zhou Y., Dong Q., Ebright Y.W., Ebright R.H.;
"Characterization of the activating region of Escherichia coli
catabolite gene activator protein (CAP). I. Saturation and alanine-
scanning mutagenesis.";
J. Mol. Biol. 243:595-602(1994).
[17]
FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 2 (AR2), INTERACTION
WITH RPOA, DNA-BINDING, DNA-BENDING, AND MUTAGENESIS OF HIS-20;
HIS-22; LYS-53; GLU-97; LYS-102; THR-159; HIS-160 AND GLY-163.
PubMed=8978616; DOI=10.1016/S0092-8674(00)81806-1;
Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.;
"Transcription activation at class II CAP-dependent promoters: two
interactions between CAP and RNA polymerase.";
Cell 87:1123-1134(1996).
[18]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[19]
FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 3 (AR3), AND
MUTAGENESIS OF 54-ASP--GLU-56 AND GLU-59.
PubMed=10860739; DOI=10.1006/jmbi.2000.3736;
Rhodius V.A., Busby S.J.;
"Transcription activation by the Escherichia coli cyclic AMP receptor
protein: determinants within activating region 3.";
J. Mol. Biol. 299:295-310(2000).
[20]
FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 3 (AR3), PROBABLE
INTERACTION WITH SIGMA-70 (RPOD), AND MUTAGENESIS OF GLU-59.
PubMed=10860740; DOI=10.1006/jmbi.2000.3737;
Rhodius V.A., Busby S.J.;
"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.";
J. Mol. Biol. 299:311-324(2000).
[21]
MUTAGENESIS OF ASP-139.
PubMed=15096034; DOI=10.1021/bi0362166;
Yu S., Lee J.C.;
"Role of residue 138 in the interdomain hinge region in transmitting
allosteric signals for DNA binding in Escherichia coli cAMP receptor
protein.";
Biochemistry 43:4662-4669(2004).
[22]
FUNCTION, REGULON, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-102
AND HIS-160.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15520470; DOI=10.1093/nar/gkh908;
Zheng D., Constantinidou C., Hobman J.L., Minchin S.D.;
"Identification of the CRP regulon using in vitro and in vivo
transcriptional profiling.";
Nucleic Acids Res. 32:5874-5893(2004).
[23]
FUNCTION, AND REGULON.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=16301522; DOI=10.1073/pnas.0506687102;
Grainger D.C., Hurd D., Harrison M., Holdstock J., Busby S.J.;
"Studies of the distribution of Escherichia coli cAMP-receptor protein
and RNA polymerase along the E. coli chromosome.";
Proc. Natl. Acad. Sci. U.S.A. 102:17693-17698(2005).
[24]
FUNCTION, AND MUTAGENESIS OF 128-THR-SER-129.
PubMed=16260780; DOI=10.1074/jbc.M509421200;
Youn H., Kerby R.L., Conrad M., Roberts G.P.;
"Study of highly constitutively active mutants suggests how cAMP
activates cAMP receptor protein.";
J. Biol. Chem. 281:1119-1127(2006).
[25]
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=19019153; DOI=10.1111/j.1365-2958.2008.06504.x;
Iwamoto A., Lemire S., Yonesaki T.;
"Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia
coli.";
Mol. Microbiol. 70:1570-1578(2008).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[27]
REVIEW.
PubMed=8394684; DOI=10.1146/annurev.bi.62.070193.003533;
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).
[28]
REVIEW.
PubMed=10550204; DOI=10.1006/jmbi.1999.3161;
Busby S., Ebright R.H.;
"Transcription activation by catabolite activator protein (CAP).";
J. Mol. Biol. 293:199-213(1999).
[29]
REVIEW.
PubMed=19439203; DOI=10.1016/j.bbapap.2009.04.015;
Won H.S., Lee Y.S., Lee S.H., Lee B.J.;
"Structural overview on the allosteric activation of cyclic AMP
receptor protein.";
Biochim. Biophys. Acta 1794:1299-1308(2009).
[30]
REVIEW ON ROLE IN CARBON CATABOLITE REPRESSION AND OTHER PROCESSES.
PubMed=22573269; DOI=10.1007/s00253-012-4101-5;
Escalante A., Salinas Cervantes A., Gosset G., Bolivar F.;
"Current knowledge of the Escherichia coli phosphoenolpyruvate-
carbohydrate phosphotransferase system: peculiarities of regulation
and impact on growth and product formation.";
Appl. Microbiol. Biotechnol. 94:1483-1494(2012).
[31]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT,
AND DOMAIN.
PubMed=6286624;
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).
[32]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT,
AND DOMAIN.
PubMed=2828639; DOI=10.1016/0022-2836(87)90315-9;
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).
[33]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-206 IN COMPLEX WITH CAMP
AND DNA, SUBUNIT, DNA-BINDING, AND DNA-BENDING.
PubMed=1653449; DOI=10.1126/science.1653449;
Schultz S., Shields G., Steitz T.A.;
"Crystal structure of a CAP-DNA complex: the DNA is bent by 90
degrees.";
Science 253:1001-1007(1991).
[34]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP
AND DNA, SUBUNIT, DNA-BINDING, AND DNA-BENDING.
PubMed=8757802; DOI=10.1006/jmbi.1996.0409;
Parkinson G., Wilson C., Gunasekera A., Ebright Y.W., Ebright R.H.,
Berman H.M.;
"Structure of the CAP-DNA complex at 2.5 angstroms resolution: a
complete picture of the protein-DNA interface.";
J. Mol. Biol. 260:395-408(1996).
[35]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH 2 CAMP PER
MONOMER AND DNA, SUBUNIT, AND DNA-BINDING.
PubMed=9096308; DOI=10.1073/pnas.94.7.2843;
Passner J.M., Steitz T.A.;
"The structure of a CAP-DNA complex having two cAMP molecules bound to
each monomer.";
Proc. Natl. Acad. Sci. U.S.A. 94:2843-2847(1997).
[36]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CAMP, AND
SUBUNIT.
PubMed=11124031; DOI=10.1006/jmbi.2000.4231;
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).
[37]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP;
DNA AND RNAP, INTERACTION WITH RPOA, DNA-BINDING, AND SUBUNIT.
PubMed=12202833; DOI=10.1126/science.1076376;
Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E.,
Ebright Y.W., Berman H.M., Ebright R.H.;
"Structural basis of transcription activation: the CAP-alpha CTD-DNA
complex.";
Science 297:1562-1566(2002).
[38]
STRUCTURE BY NMR OF 2-210 OF APO-CRP, ENZYME REGULATION, AND SUBUNIT.
PubMed=19359484; DOI=10.1073/pnas.0900595106;
Popovych N., Tzeng S.R., Tonelli M., Ebright R.H., Kalodimos C.G.;
"Structural basis for cAMP-mediated allosteric control of the
catabolite activator protein.";
Proc. Natl. Acad. Sci. U.S.A. 106:6927-6932(2009).
[39]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APO-CRP, ENZYME REGULATION,
SUBUNIT, AND MUTAGENESIS OF ASP-139.
PubMed=19805344; DOI=10.1073/pnas.0908380106;
Sharma H., Yu S., Kong J., Wang J., Steitz T.A.;
"Structure of apo-CAP reveals that large conformational changes are
necessary for DNA binding.";
Proc. Natl. Acad. Sci. U.S.A. 106:16604-16609(2009).
[40]
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, AND SUBUNIT.
PubMed=19903881; DOI=10.1073/pnas.0908782106;
Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M.,
Arnold E., Ebright R.H., Lawson C.L.;
"Three-dimensional EM structure of an intact activator-dependent
transcription initiation complex.";
Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009).
[41]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-210 IN COMPLEX WITH 2 CAMP
PER MONOMER, AND SUBUNIT.
Kumarevel T.S., Tanaka T., Shinkai A., Yokoyama S.;
"Crystal structure of activated CRP protein from E.coli.";
Submitted (FEB-2009) to the PDB data bank.
[42]
STRUCTURE BY NMR OF 2-210 OF APO-CRP, AND MUTAGENESIS OF
128-THR-SER-129.
PubMed=23644478; DOI=10.1038/nchembio.1250;
Tzeng S.R., Kalodimos C.G.;
"Allosteric inhibition through suppression of transient conformational
states.";
Nat. Chem. Biol. 9:462-465(2013).
-!- 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
(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). {ECO:0000269|PubMed:10860739,
ECO:0000269|PubMed:10860740, ECO:0000269|PubMed:15520470,
ECO:0000269|PubMed:16260780, ECO:0000269|PubMed:16301522,
ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:2982847,
ECO:0000269|PubMed:7966284, ECO:0000269|PubMed:8392187,
ECO:0000269|PubMed:8978616}.
-!- 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.
{ECO:0000269|PubMed:19359484, ECO:0000269|PubMed:19805344}.
-!- SUBUNIT: 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).
{ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:19359484, ECO:0000269|PubMed:19805344,
ECO:0000269|PubMed:19903881, ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:2839152, ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802, ECO:0000269|PubMed:8978616,
ECO:0000269|PubMed:9096308, ECO:0000269|Ref.41}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-547513, EBI-547513;
P0AFG0:nusG; NbExp=2; IntAct=EBI-547513, EBI-369628;
P23862:priC; NbExp=2; IntAct=EBI-547513, EBI-1117383;
P0A7K2:rplL; NbExp=2; IntAct=EBI-547513, EBI-543702;
P0A8E5:yacL; NbExp=4; IntAct=EBI-547513, EBI-554965;
-!- 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 (PubMed:1328816) and negatively autoregulated
(PubMed:6297782). {ECO:0000269|PubMed:1328816,
ECO:0000269|PubMed:19019153, ECO:0000269|PubMed:6297782}.
-!- DOMAIN: The N-terminal domain binds cAMP and is responsible for
homodimerization, while the C-terminal domain binds DNA when cAMP
is bound. {ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624}.
-!- DISRUPTION PHENOTYPE: Not essential (on rich medium), greatly
increased levels of cAMP. Eliminates the NaCl sensitivity of an
rnlA deletion mutant. {ECO:0000269|PubMed:15520470,
ECO:0000269|PubMed:164435, ECO:0000269|PubMed:19019153}.
-!- MISCELLANEOUS: Binds 2 cAMP; cAMP 1 is in the anti conformation,
while cAMP 2 is in the syn conformation.
{ECO:0000305|PubMed:9096308}.
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EMBL; J01598; AAA23601.1; -; Genomic_DNA.
EMBL; U18997; AAA58154.1; -; Genomic_DNA.
EMBL; U00096; AAC76382.1; -; Genomic_DNA.
EMBL; AP009048; BAE77933.1; -; Genomic_DNA.
PIR; A93416; QRECC.
RefSeq; NP_417816.1; NC_000913.3.
RefSeq; WP_000242755.1; NZ_CP014272.1.
PDB; 1CGP; X-ray; 3.00 A; A/B=2-206.
PDB; 1G6N; X-ray; 2.10 A; A/B=1-210.
PDB; 1HW5; X-ray; 1.82 A; A/B=1-210.
PDB; 1I5Z; X-ray; 1.90 A; A/B=2-210.
PDB; 1I6X; X-ray; 2.20 A; A/B=2-210.
PDB; 1J59; X-ray; 2.50 A; A/B=2-210.
PDB; 1LB2; X-ray; 3.10 A; A=2-210.
PDB; 1O3Q; X-ray; 3.00 A; A=9-208.
PDB; 1O3R; X-ray; 3.00 A; A=9-208.
PDB; 1O3S; X-ray; 3.00 A; A=9-208.
PDB; 1O3T; X-ray; 2.80 A; A/B=9-208.
PDB; 1RUN; X-ray; 2.70 A; A/B=2-210.
PDB; 1RUO; X-ray; 2.70 A; A/B=2-210.
PDB; 1ZRC; X-ray; 2.80 A; A/B=2-210.
PDB; 1ZRD; X-ray; 2.80 A; A/B=2-210.
PDB; 1ZRE; X-ray; 2.80 A; A/B=2-210.
PDB; 1ZRF; X-ray; 2.10 A; A/B=2-210.
PDB; 2CGP; X-ray; 2.20 A; A=1-210.
PDB; 2GAP; Model; -; A/B=2-209.
PDB; 2GZW; X-ray; 2.21 A; A/B/C/D=2-210.
PDB; 2WC2; NMR; -; A/B=2-210.
PDB; 3FWE; X-ray; 2.30 A; A/B=1-210.
PDB; 3HIF; X-ray; 3.59 A; A/B/C/D/E/F=1-210.
PDB; 3IYD; EM; -; G/H=2-210.
PDB; 3KCC; X-ray; 1.66 A; A/B=1-210.
PDB; 3N4M; X-ray; 2.99 A; A=2-210.
PDB; 3QOP; X-ray; 1.96 A; A/B=1-210.
PDB; 3RDI; X-ray; 2.95 A; A/B=1-210.
PDB; 3ROU; X-ray; 2.10 A; A/B=1-210.
PDB; 3RPQ; X-ray; 2.61 A; A/B=1-210.
PDB; 3RYP; X-ray; 1.60 A; A/B=1-210.
PDB; 3RYR; X-ray; 2.70 A; A/B=1-210.
PDB; 4BH9; NMR; -; A=2-210.
PDB; 4BHP; NMR; -; A=2-210.
PDB; 4FT8; X-ray; 1.97 A; A/B=2-210.
PDB; 4HZF; X-ray; 1.48 A; A/B=1-210.
PDB; 4I01; X-ray; 2.30 A; A/B=1-210.
PDB; 4I02; X-ray; 1.75 A; A/B/C/D/E/F=1-210.
PDB; 4I09; X-ray; 2.05 A; A/B=1-210.
PDB; 4I0A; X-ray; 2.20 A; A/B=1-210.
PDB; 4I0B; X-ray; 1.50 A; A/B=1-210.
PDB; 4R8H; X-ray; 1.46 A; A/B=1-210.
PDB; 5CIZ; X-ray; 5.01 A; A=2-210.
PDBsum; 1CGP; -.
PDBsum; 1G6N; -.
PDBsum; 1HW5; -.
PDBsum; 1I5Z; -.
PDBsum; 1I6X; -.
PDBsum; 1J59; -.
PDBsum; 1LB2; -.
PDBsum; 1O3Q; -.
PDBsum; 1O3R; -.
PDBsum; 1O3S; -.
PDBsum; 1O3T; -.
PDBsum; 1RUN; -.
PDBsum; 1RUO; -.
PDBsum; 1ZRC; -.
PDBsum; 1ZRD; -.
PDBsum; 1ZRE; -.
PDBsum; 1ZRF; -.
PDBsum; 2CGP; -.
PDBsum; 2GAP; -.
PDBsum; 2GZW; -.
PDBsum; 2WC2; -.
PDBsum; 3FWE; -.
PDBsum; 3HIF; -.
PDBsum; 3IYD; -.
PDBsum; 3KCC; -.
PDBsum; 3N4M; -.
PDBsum; 3QOP; -.
PDBsum; 3RDI; -.
PDBsum; 3ROU; -.
PDBsum; 3RPQ; -.
PDBsum; 3RYP; -.
PDBsum; 3RYR; -.
PDBsum; 4BH9; -.
PDBsum; 4BHP; -.
PDBsum; 4FT8; -.
PDBsum; 4HZF; -.
PDBsum; 4I01; -.
PDBsum; 4I02; -.
PDBsum; 4I09; -.
PDBsum; 4I0A; -.
PDBsum; 4I0B; -.
PDBsum; 4R8H; -.
PDBsum; 5CIZ; -.
ProteinModelPortal; P0ACJ8; -.
SMR; P0ACJ8; -.
DIP; DIP-29232N; -.
IntAct; P0ACJ8; 43.
MINT; MINT-1249660; -.
STRING; 316385.ECDH10B_3533; -.
DrugBank; DB02527; Cyclic Adenosine Monophosphate.
iPTMnet; P0ACJ8; -.
PaxDb; P0ACJ8; -.
PRIDE; P0ACJ8; -.
EnsemblBacteria; AAC76382; AAC76382; b3357.
EnsemblBacteria; BAE77933; BAE77933; BAE77933.
GeneID; 29925187; -.
GeneID; 947867; -.
KEGG; ecj:JW5702; -.
KEGG; eco:b3357; -.
PATRIC; fig|1411691.4.peg.3373; -.
EchoBASE; EB0162; -.
EcoGene; EG10164; crp.
eggNOG; COG0664; LUCA.
HOGENOM; HOG000250565; -.
InParanoid; P0ACJ8; -.
KO; K10914; -.
PhylomeDB; P0ACJ8; -.
BioCyc; EcoCyc:PD00257; -.
EvolutionaryTrace; P0ACJ8; -.
PRO; PR:P0ACJ8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
CollecTF; EXPREG_00000850; -.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0045013; P:carbon catabolite repression of transcription; IMP:EcoCyc.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoliWiki.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoliWiki.
GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
CDD; cd00038; CAP_ED; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR012318; HTH_CRP.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00325; Crp; 1.
PRINTS; PR00034; HTHCRP.
SMART; SM00100; cNMP; 1.
SMART; SM00419; HTH_CRP; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS00888; CNMP_BINDING_1; 1.
PROSITE; PS00889; CNMP_BINDING_2; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS00042; HTH_CRP_1; 1.
PROSITE; PS51063; HTH_CRP_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; cAMP; cAMP-binding;
Complete proteome; Direct protein sequencing; DNA-binding;
Nucleotide-binding; Reference proteome; Repressor; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17895580}.
CHAIN 2 210 cAMP-activated global transcriptional
regulator CRP.
/FTId=PRO_0000100144.
DOMAIN 138 210 HTH crp-type. {ECO:0000255|PROSITE-
ProRule:PRU00387}.
NP_BIND 57 63 cAMP 1. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
NP_BIND 72 74 cAMP 1. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
NP_BIND 83 84 cAMP 1. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
NP_BIND 128 129 cAMP 1. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
NP_BIND 136 137 cAMP 2. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
NP_BIND 171 181 cAMP 2. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
DNA_BIND 180 186 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00387}.
REGION 20 22 Activating region 2 (AR2); probably
contacts the N-terminus of RpoA.
REGION 53 59 Activating region 3 (AR3); probably
contacts sigma-70 (RpoD).
REGION 154 163 Activating region 1 (AR1); probably
contacts the C-terminus of RpoA.
BINDING 129 129 cAMP. {ECO:0000269|PubMed:11124031,
ECO:0000269|PubMed:12202833,
ECO:0000269|PubMed:1653449,
ECO:0000269|PubMed:2828639,
ECO:0000269|PubMed:6286624,
ECO:0000269|PubMed:8757802}.
SITE 97 97 Activating region 2 (AR2); probably
contacts the N-terminus of RpoA.
SITE 102 102 Activating region 2 (AR2); probably
contacts the N-terminus of RpoA.
MOD_RES 101 101 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MUTAGEN 20 20 H->A,L,Y: Decreased transcription
activation at class II promoters,
decreased interaction with RNAP, binds
DNA. {ECO:0000269|PubMed:8978616}.
MUTAGEN 22 22 H->A,L: Decreased transcription
activation at class II promoters,
decreased interaction with RNAP, binds
DNA. {ECO:0000269|PubMed:8978616}.
MUTAGEN 53 53 K->N: Increased activation at class II
promoters, increased interaction with
RNAP. {ECO:0000269|PubMed:8978616}.
MUTAGEN 54 56 DEE->AAA: 80% reduction in activation of
class II promoters; 95% loss when
associated with A-59.
{ECO:0000269|PubMed:10860739}.
MUTAGEN 59 59 E->A: 45% reduction in activation of
class II promoters; 95% loss when
associated with AAA-54-56.
{ECO:0000269|PubMed:10860739,
ECO:0000269|PubMed:10860740}.
MUTAGEN 59 59 E->G,K: Reduction in activation of class
II promoters.
{ECO:0000269|PubMed:10860739,
ECO:0000269|PubMed:10860740}.
MUTAGEN 63 63 S->A: Enhanced cAMP-binding, enhanced
transcription.
{ECO:0000269|PubMed:2845936}.
MUTAGEN 83 83 R->L: Loss of cAMP-binding.
{ECO:0000269|PubMed:2845936}.
MUTAGEN 84 84 S->A,K: No modification of cAMP-binding.
{ECO:0000269|PubMed:2845936}.
MUTAGEN 97 97 E->A: Increased transcription activation
at class II promoters, binds DNA.
{ECO:0000269|PubMed:8978616}.
MUTAGEN 102 102 K->E: Disrupts AR2. No activation of
class II promoters, decreased interaction
with RNAP, binds DNA.
{ECO:0000269|PubMed:15520470,
ECO:0000269|PubMed:8978616}.
MUTAGEN 128 129 TS->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. {ECO:0000269|PubMed:16260780,
ECO:0000269|PubMed:23644478}.
MUTAGEN 128 128 T->A: No modification of cAMP-binding.
{ECO:0000269|PubMed:2845936}.
MUTAGEN 129 129 S->A: Reduced DNA-binding; no
modification of cAMP-binding.
{ECO:0000269|PubMed:2845936,
ECO:0000269|PubMed:3333845}.
MUTAGEN 139 139 D->L: Some stabilization of an inactive
(apo-) form. Decreased affinity for DNA,
normal subunit association.
{ECO:0000269|PubMed:15096034,
ECO:0000269|PubMed:19805344,
ECO:0000269|PubMed:8380500}.
MUTAGEN 157 157 A->D,P: Decreased transcription
activation (6-29%), binds DNA.
{ECO:0000269|PubMed:7966284,
ECO:0000269|PubMed:8392187}.
MUTAGEN 159 159 T->A,I,N,S,V: Decreased transcription
activation (15-87%) at class I and II
promoters, binds DNA.
{ECO:0000269|PubMed:7966284,
ECO:0000269|PubMed:8392187,
ECO:0000269|PubMed:8978616}.
MUTAGEN 160 160 H->A,K,L,N,P,Q,R,Y: Disrupts AR1.
Decreased transcription activation (3-
45%) at class I and II promoters, binds
DNA. {ECO:0000269|PubMed:15520470,
ECO:0000269|PubMed:7966284,
ECO:0000269|PubMed:8392187,
ECO:0000269|PubMed:8978616}.
MUTAGEN 163 163 G->A,C,D,R,S,V: Decreased transcription
activation (2-62%) at class I and II
promoters, binds DNA.
{ECO:0000269|PubMed:7966284,
ECO:0000269|PubMed:8392187,
ECO:0000269|PubMed:8978616}.
MUTAGEN 181 181 R->K: Suppresses DNA-binding.
{ECO:0000269|PubMed:3333845}.
MUTAGEN 181 181 R->L: Suppresses DNA-binding.
{ECO:0000269|PubMed:3333845}.
MUTAGEN 186 186 R->K: No modification of DNA-binding.
{ECO:0000269|PubMed:3333845}.
MUTAGEN 186 186 R->L: Marginally reduced DNA-binding.
{ECO:0000269|PubMed:3333845}.
CONFLICT 29 29 T -> K (in Ref. 4; BAE77933).
{ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:2WC2}.
HELIX 10 16 {ECO:0000244|PDB:4R8H}.
STRAND 19 24 {ECO:0000244|PDB:4R8H}.
STRAND 25 27 {ECO:0000244|PDB:2WC2}.
STRAND 29 31 {ECO:0000244|PDB:4R8H}.
STRAND 33 36 {ECO:0000244|PDB:1O3T}.
STRAND 39 45 {ECO:0000244|PDB:4R8H}.
STRAND 47 53 {ECO:0000244|PDB:4R8H}.
STRAND 55 57 {ECO:0000244|PDB:1HW5}.
STRAND 59 66 {ECO:0000244|PDB:4R8H}.
STRAND 70 72 {ECO:0000244|PDB:4R8H}.
HELIX 74 77 {ECO:0000244|PDB:4R8H}.
STRAND 78 80 {ECO:0000244|PDB:1I5Z}.
STRAND 85 91 {ECO:0000244|PDB:4R8H}.
STRAND 93 99 {ECO:0000244|PDB:4R8H}.
HELIX 100 109 {ECO:0000244|PDB:4R8H}.
HELIX 112 137 {ECO:0000244|PDB:4R8H}.
HELIX 140 152 {ECO:0000244|PDB:4R8H}.
STRAND 154 156 {ECO:0000244|PDB:1J59}.
STRAND 158 160 {ECO:0000244|PDB:4R8H}.
STRAND 163 167 {ECO:0000244|PDB:4R8H}.
HELIX 170 177 {ECO:0000244|PDB:4R8H}.
HELIX 181 193 {ECO:0000244|PDB:4R8H}.
STRAND 196 200 {ECO:0000244|PDB:4R8H}.
STRAND 203 207 {ECO:0000244|PDB:4R8H}.
SEQUENCE 210 AA; 23640 MW; DCBC24FA46C61B3D CRC64;
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV LIKDEEGKEM
ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY KKFRQLIQVN PDILMRLSAQ
MARRLQVTSE KVGNLAFLDV TGRIAQTLLN LAKQPDAMTH PDGMQIKITR QEIGQIVGCS
RETVGRILKM LEDQNLISAH GKTIVVYGTR


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