Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0ACJ8 (CRP_ECOLI)

Protein

cAMP-activated global transcriptional regulator CRP

Gene

crp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).10 Publications

Miscellaneous

Binds 2 cAMP; cAMP 1 is in the anti conformation, while cAMP 2 is in the syn conformation.1 Publication

Activity regulationi

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei97Activating region 2 (AR2); probably contacts the N-terminus of RpoA1
Sitei102Activating region 2 (AR2); probably contacts the N-terminus of RpoA1
Binding sitei129cAMP6 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi57 – 63cAMP 16 Publications7
Nucleotide bindingi72 – 74cAMP 16 Publications3
Nucleotide bindingi83 – 84cAMP 16 Publications2
Nucleotide bindingi128 – 129cAMP 16 Publications2
Nucleotide bindingi136 – 137cAMP 26 Publications2
Nucleotide bindingi171 – 181cAMP 26 PublicationsAdd BLAST11
DNA bindingi180 – 186H-T-H motifPROSITE-ProRule annotation7

GO - Molecular functioni

  • cAMP binding Source: UniProtKB-KW
  • DNA-binding transcription factor activity Source: GO_Central
  • identical protein binding Source: IntAct
  • sequence-specific DNA binding Source: CollecTF
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandcAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00257

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:crp
Synonyms:cap, csm
Ordered Locus Names:b3357, JW5702
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10164 crp

Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Pathology & Biotechi

Disruption phenotypei

Not essential (on rich medium), greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20H → A, L or Y: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication1
Mutagenesisi22H → A or L: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication1
Mutagenesisi53K → N: Increased activation at class II promoters, increased interaction with RNAP. 1 Publication1
Mutagenesisi54 – 56DEE → AAA: 80% reduction in activation of class II promoters; 95% loss when associated with A-59. 1 Publication3
Mutagenesisi59E → A: 45% reduction in activation of class II promoters; 95% loss when associated with AAA-54-56. 2 Publications1
Mutagenesisi59E → G or K: Reduction in activation of class II promoters. 2 Publications1
Mutagenesisi63S → A: Enhanced cAMP-binding, enhanced transcription. 1 Publication1
Mutagenesisi83R → L: Loss of cAMP-binding. 1 Publication1
Mutagenesisi84S → A or K: No modification of cAMP-binding. 1 Publication1
Mutagenesisi97E → A: Increased transcription activation at class II promoters, binds DNA. 1 Publication1
Mutagenesisi102K → E: Disrupts AR2. No activation of class II promoters, decreased interaction with RNAP, binds DNA. 2 Publications1
Mutagenesisi128 – 129TS → 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. 2 Publications2
Mutagenesisi128T → A: No modification of cAMP-binding. 1 Publication1
Mutagenesisi129S → A: Reduced DNA-binding; no modification of cAMP-binding. 2 Publications1
Mutagenesisi139D → L: Some stabilization of an inactive (apo-) form. Decreased affinity for DNA, normal subunit association. 3 Publications1
Mutagenesisi157A → D or P: Decreased transcription activation (6-29%), binds DNA. 2 Publications1
Mutagenesisi159T → A, I, N, S or V: Decreased transcription activation (15-87%) at class I and II promoters, binds DNA. 3 Publications1
Mutagenesisi160H → A, K, L, N, P, Q, R or Y: Disrupts AR1. Decreased transcription activation (3-45%) at class I and II promoters, binds DNA. 4 Publications1
Mutagenesisi163G → A, C, D, R, S or V: Decreased transcription activation (2-62%) at class I and II promoters, binds DNA. 3 Publications1
Mutagenesisi181R → K: Suppresses DNA-binding. 1 Publication1
Mutagenesisi181R → L: Suppresses DNA-binding. 1 Publication1
Mutagenesisi186R → K: No modification of DNA-binding. 1 Publication1
Mutagenesisi186R → L: Marginally reduced DNA-binding. 1 Publication1

Chemistry databases

DrugBankiDB02527 Cyclic Adenosine Monophosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001001442 – 210cAMP-activated global transcriptional regulator CRPAdd BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0ACJ8
PaxDbiP0ACJ8
PRIDEiP0ACJ8

PTM databases

iPTMnetiP0ACJ8

Expressioni

Inductioni

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).3 Publications

Gene expression databases

CollecTFiEXPREG_00000850

Interactioni

Subunit structurei

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).14 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi4262928, 15 interactors
DIPiDIP-29232N
IntActiP0ACJ8, 42 interactors
MINTiP0ACJ8
STRINGi316385.ECDH10B_3533

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0ACJ8
SMRiP0ACJ8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACJ8

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini138 – 210HTH crp-typePROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 22Activating region 2 (AR2); probably contacts the N-terminus of RpoA3
Regioni53 – 59Activating region 3 (AR3); probably contacts sigma-70 (RpoD)7
Regioni154 – 163Activating region 1 (AR1); probably contacts the C-terminus of RpoA10

Domaini

The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound.2 Publications

Phylogenomic databases

eggNOGiCOG0664 LUCA
HOGENOMiHOG000250565
InParanoidiP0ACJ8
KOiK10914
PhylomeDBiP0ACJ8

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di1.10.10.10, 1 hit
2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR018490 cNMP-bd-like
IPR018488 cNMP-bd_CS
IPR000595 cNMP-bd_dom
IPR012318 HTH_CRP
IPR014710 RmlC-like_jellyroll
IPR018335 Tscrpt_reg_HTH_Crp-type_CS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00027 cNMP_binding, 1 hit
PF00325 Crp, 1 hit
PRINTSiPR00034 HTHCRP
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SM00419 HTH_CRP, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF51206 SSF51206, 1 hit
PROSITEiView protein in 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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ACJ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV 
        60         70         80         90        100
LIKDEEGKEM ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY 
       110        120        130        140        150
KKFRQLIQVN PDILMRLSAQ MARRLQVTSE KVGNLAFLDV TGRIAQTLLN 
       160        170        180        190        200
LAKQPDAMTH PDGMQIKITR QEIGQIVGCS RETVGRILKM LEDQNLISAH 
       210
GKTIVVYGTR
Length:210
Mass (Da):23,640
Last modified:July 21, 1986 - v1
Checksum:iDCBC24FA46C61B3D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29T → K in BAE77933 (PubMed:16738553).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01598 Genomic DNA Translation: AAA23601.1
U18997 Genomic DNA Translation: AAA58154.1
U00096 Genomic DNA Translation: AAC76382.1
AP009048 Genomic DNA Translation: BAE77933.1
PIRiA93416 QRECC
RefSeqiNP_417816.1, NC_000913.3
WP_000242755.1, NZ_CP014272.1

Genome annotation databases

EnsemblBacteriaiAAC76382; AAC76382; b3357
BAE77933; BAE77933; BAE77933
GeneIDi33939152
947867
KEGGiecj:JW5702
eco:b3357
PATRICifig|1411691.4.peg.3373

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01598 Genomic DNA Translation: AAA23601.1
U18997 Genomic DNA Translation: AAA58154.1
U00096 Genomic DNA Translation: AAC76382.1
AP009048 Genomic DNA Translation: BAE77933.1
PIRiA93416 QRECC
RefSeqiNP_417816.1, NC_000913.3
WP_000242755.1, NZ_CP014272.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4R8HX-ray1.46A/B1-210[»]
5CIZX-ray5.01A2-210[»]
ProteinModelPortaliP0ACJ8
SMRiP0ACJ8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262928, 15 interactors
DIPiDIP-29232N
IntActiP0ACJ8, 42 interactors
MINTiP0ACJ8
STRINGi316385.ECDH10B_3533

Chemistry databases

DrugBankiDB02527 Cyclic Adenosine Monophosphate

PTM databases

iPTMnetiP0ACJ8

Proteomic databases

EPDiP0ACJ8
PaxDbiP0ACJ8
PRIDEiP0ACJ8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76382; AAC76382; b3357
BAE77933; BAE77933; BAE77933
GeneIDi33939152
947867
KEGGiecj:JW5702
eco:b3357
PATRICifig|1411691.4.peg.3373

Organism-specific databases

EchoBASEiEB0162
EcoGeneiEG10164 crp

Phylogenomic databases

eggNOGiCOG0664 LUCA
HOGENOMiHOG000250565
InParanoidiP0ACJ8
KOiK10914
PhylomeDBiP0ACJ8

Enzyme and pathway databases

BioCyciEcoCyc:PD00257

Miscellaneous databases

EvolutionaryTraceiP0ACJ8
PROiPR:P0ACJ8

Gene expression databases

CollecTFiEXPREG_00000850

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di1.10.10.10, 1 hit
2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR018490 cNMP-bd-like
IPR018488 cNMP-bd_CS
IPR000595 cNMP-bd_dom
IPR012318 HTH_CRP
IPR014710 RmlC-like_jellyroll
IPR018335 Tscrpt_reg_HTH_Crp-type_CS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00027 cNMP_binding, 1 hit
PF00325 Crp, 1 hit
PRINTSiPR00034 HTHCRP
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SM00419 HTH_CRP, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF51206 SSF51206, 1 hit
PROSITEiView protein in 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
ProtoNetiSearch...

Entry informationi

Entry nameiCRP_ECOLI
AccessioniPrimary (citable) accession number: P0ACJ8
Secondary accession number(s): P03020, Q2M723
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 7, 2018
This is version 118 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again