P0ACJ8 (CRP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP receptor protein
Short name=Crp

Alternative name(s):
Catabolite gene activator
Short name=CAP
cAMP regulatory protein

Gene names

Name:	crp
Synonyms:	cap, csm
Ordered Locus Names:	b3357, JW5702

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 as well as for adenylate cyclase (cyaA), which generates cAMP. Ref.6
Subunit structure	Binds DNA as a dimer.
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). Ref.9
Disruption phenotype	Not essential, greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant. Ref.9
Sequence similarities	Contains 1 cyclic nucleotide-binding domain. Contains 1 HTH crp-type DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	DNA-binding Nucleotide-binding cAMP cAMP-binding
Molecular function	Activator Repressor
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbon catabolite repression of transcription Inferred from mutant phenotype PubMed 16838379. Source: EcoCyc positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 15520470. Source: EcoliWiki transcription, DNA-dependent Inferred from direct assay PubMed 10760178PubMed 11742992PubMed 12923087PubMed 16166533PubMed 7551052. Source: EcoCyc
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplL	P0A7K2	1	EBI-547513,EBI-543702

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 210

209

cAMP receptor protein

PRO_0000100144

Regions

Domain

138 – 210

73

HTH crp-type

Nucleotide binding

10 – 133

124

cAMP

DNA binding

170 – 189

20

H-T-H motif Ref.6

Sites

Binding site

129

1

cAMP

Amino acid modifications

Modified residue

101

1

N6-acetyllysine Ref.8

Experimental info

Mutagenesis

63

1

S → A: Enhanced cAMP-binding.

Mutagenesis

83

1

R → L: Loss of cAMP-binding.

Mutagenesis

84

1

S → A or K: No modification of cAMP-binding.

Mutagenesis

128

1

T → A: No modification of cAMP-binding.

Mutagenesis

129

1

S → A: Reduced DNA-binding; no modification of cAMP-binding.

Mutagenesis

181

1

R → K: Suppresses DNA-binding.

Mutagenesis

181

1

R → L: Suppresses DNA-binding.

Mutagenesis

186

1

R → K: No modification of DNA-binding.

Mutagenesis

186

1

R → L: Marginally reduced DNA-binding.

Sequence conflict

29

1

T → K in BAE77933. Ref.4

Secondary structure

1

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210

Helix Strand Turn

Details...

Helix

10 – 16

7

Beta strand

19 – 24

6

Beta strand

29 – 31

3

Beta strand

33 – 36

4

Beta strand

39 – 53

15

Beta strand

55 – 57

3

Beta strand

59 – 66

8

Beta strand

70 – 72

3

Turn

74 – 77

4

Beta strand

78 – 80

3

Beta strand

84 – 91

8

Beta strand

93 – 99

7

Helix

100 – 109

10

Helix

112 – 137

26

Helix

140 – 151

12

Beta strand

154 – 156

3

Beta strand

158 – 160

3

Beta strand

163 – 167

5

Helix

170 – 177

8

Helix

181 – 193

13

Beta strand

196 – 200

5

Beta strand

203 – 207

5

Sequences

	Sequence		Length	Mass (Da)
	P0ACJ8 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: DCBC24FA46C61B3D	FASTA	210	23,640
	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

References

	« Hide 'large scale' referencesShow '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].
[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 277:1453-1474(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]	"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 REPRESSOR, DNA-BINDING.
[7]	"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.
[8]	"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.
[9]	"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.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: REVIEW.
[13]	"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).
[14]	"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).
[15]	"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) IN COMPLEX WITH DNA.
[16]	"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).
+	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.

PIR

QRECC. A93416.

RefSeq

NP_417816.1. NC_000913.2.
YP_492074.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	[»]

ProteinModelPortal

P0ACJ8.

SMR

P0ACJ8. Positions 8-209.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29232N.

IntAct

P0ACJ8. 8 interactions.

MINT

MINT-1249660.

STRING

511145.b3357.

Proteomic databases

PaxDb

P0ACJ8.

PRIDE

P0ACJ8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76382; AAC76382; b3357.
BAE77933; BAE77933; BAE77933.

GeneID

12933934.
947867.

KEGG

ecj:Y75_p3818.
eco:b3357.

PATRIC

32122148. VBIEscCol129921_3451.

Organism-specific databases

EchoBASE

EB0162.

EcoGene

EG10164. crp.

Phylogenomic databases

eggNOG

COG0664.

HOGENOM

HOG000250565.

KO

K10914.

OMA

YLNNGDF.

ProtClustDB

PRK11753.

Enzyme and pathway databases

BioCyc

EcoCyc:PD00257.
ECOL316407:JW5702-MONOMER.

Gene expression databases

Genevestigator

P0ACJ8.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
2.60.120.10. 1 hit.

InterPro

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]

Pfam

PF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view]

PRINTS

PR00034. HTHCRP.

SMART

SM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view]

SUPFAM

SSF51206. cNMP_binding. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ACJ8.

Entry information

Entry name

CRP_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program