P0ACJ8 (CRP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
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.
Subunit structure	Binds DNA as a dimer.
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
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
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

Chain

1 – 210

210

Catabolite gene activator

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

Sites

Binding site

129

1

cAMP

Amino acid modifications

Modified residue

101

1

N6-acetyllysine Ref.5

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

39 – 46

8

Beta strand

48 – 53

6

Beta strand

59 – 65

7

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

161 – 166

6

Helix

170 – 177

8

Helix

181 – 193

13

Beta strand

196 – 200

5

Beta strand

203 – 206

4

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: 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.

PIR

QRECC. A93416.

RefSeq

NP_417816.1. NC_000913.2.

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	[»]

ProteinModelPortal

P0ACJ8.

SMR

P0ACJ8. Positions 2-208.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29232N.

IntAct

P0ACJ8. 8 interactions.

MINT

MINT-1249660.

2D gel databases

ECO2DBASE

I021.4. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004831; EBESCP00000004831; EBESCG00000003945.
EBESCT00000004832; EBESCP00000004832; EBESCG00000003945.
EBESCT00000004833; EBESCP00000004833; EBESCG00000003945.
EBESCT00000017422; EBESCP00000016713; EBESCG00000016478.

GeneID

947867.

GenomeReviews

Gene locus JW5702 in contig AP009048_GR.
Gene locus b3357 in contig U00096_GR.

KEGG

ecj:JW5702.
eco:b3357.

PATRIC

32122148. VBIEscCol129921_3451.

Organism-specific databases

EchoBASE

EB0162.

EcoGene

EG10164. crp.

Phylogenomic databases

eggNOG

COG0664.

GeneTree

EBGT00050000009957.

HOGENOM

HBG648099.

OMA

RAKSACE.

PhylomeDB

P0ACJ8.

ProtClustDB

PRK11753.

Enzyme and pathway databases

BioCyc

EcoCyc:PD00257.

Gene expression databases

Genevestigator

P0ACJ8.

Family and domain databases

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_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K10914.

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...

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:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program