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Protein

Carbon storage regulator

Gene

csrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to mRNA to regulate post-transcriptional activity. Affects glycogen biosynthesis, gluconeogenesis, cell size and surface properties. Regulates glycogen synthesis under both aerobic and anaerobic conditions. Seems to accelerate the degradation of glg gene transcripts, potentially through selective RNA binding. Acts to inhibit interaction between the LetD protein and the A subunit of DNA gyrase. Also required for motility and flagellum biosynthesis through the post-transcriptional activation of flhDC expression. This involves binding to and stabilization of the flhDC message by CsrA. Binds to and reduces levels of probable diguanylate cyclases ycdT and ydeH.3 Publications

GO - Molecular functioni

  • mRNA 5'-UTR binding Source: EcoCyc

GO - Biological processi

  • mRNA catabolic process Source: UniProtKB-HAMAP
  • negative regulation of glycogen biosynthetic process Source: EcoCyc
  • negative regulation of translational initiation Source: EcoCyc
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11447-MONOMER.
ECOL316407:JW2666-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon storage regulator
Gene namesi
Name:csrA
Synonyms:zfiA
Ordered Locus Names:b2696, JW2666
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11447. csrA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Allows basal levels of poly-GlcNAc synthesis and biofilm formation; serves as a model system for biofilm formation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6161Carbon storage regulatorPRO_0000177061Add
BLAST

Proteomic databases

EPDiP69913.
PaxDbiP69913.
PRIDEiP69913.

Expressioni

Inductioni

Activated by MqsR.2 Publications

Interactioni

Subunit structurei

Homodimer. Binds to and is sequestered by the non-coding RNAs CsrB and CsrC which antagonize the activity of CsrA.1 Publication

Protein-protein interaction databases

BioGridi4259421. 213 interactions.
DIPiDIP-47836N.
IntActiP69913. 8 interactions.
MINTiMINT-1317679.
STRINGi511145.b2696.

Structurei

Secondary structure

1
61
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi12 – 176Combined sources
Beta strandi19 – 213Combined sources
Beta strandi27 – 359Combined sources
Beta strandi38 – 436Combined sources
Helixi46 – 516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y00NMR-A/B1-61[»]
ProteinModelPortaliP69913.
SMRiP69913. Positions 1-57.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69913.

Family & Domainsi

Sequence similaritiesi

Belongs to the CsrA family.Curated

Phylogenomic databases

eggNOGiCOG1551. LUCA.
HOGENOMiHOG000020767.
InParanoidiP69913.
KOiK03563.
OMAiIYARIQR.
OrthoDBiEOG6DC6PM.
PhylomeDBiP69913.

Family and domain databases

HAMAPiMF_00167. CsrA.
InterProiIPR003751. CsrA.
[Graphical view]
PfamiPF02599. CsrA. 1 hit.
[Graphical view]
ProDomiPD009007. CsrA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR00202. csrA. 1 hit.

Sequencei

Sequence statusi: Complete.

P69913-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLILTRRVGE TLMIGDEVTV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR
60
IQAEKSQQSS Y
Length:61
Mass (Da):6,856
Last modified:January 4, 2005 - v1
Checksum:i16308FC572670E1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07596 Unassigned DNA. Translation: AAA71919.1.
D44453 Genomic DNA. Translation: BAA21555.1.
U00096 Genomic DNA. Translation: AAC75738.1.
AP009048 Genomic DNA. Translation: BAA16558.1.
PIRiB40608.
RefSeqiNP_417176.1. NC_000913.3.
WP_000906486.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75738; AAC75738; b2696.
BAA16558; BAA16558; BAA16558.
GeneIDi5551697.
947176.
KEGGiecj:JW2666.
eco:b2696.
PATRICi32120786. VBIEscCol129921_2785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07596 Unassigned DNA. Translation: AAA71919.1.
D44453 Genomic DNA. Translation: BAA21555.1.
U00096 Genomic DNA. Translation: AAC75738.1.
AP009048 Genomic DNA. Translation: BAA16558.1.
PIRiB40608.
RefSeqiNP_417176.1. NC_000913.3.
WP_000906486.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y00NMR-A/B1-61[»]
ProteinModelPortaliP69913.
SMRiP69913. Positions 1-57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259421. 213 interactions.
DIPiDIP-47836N.
IntActiP69913. 8 interactions.
MINTiMINT-1317679.
STRINGi511145.b2696.

Proteomic databases

EPDiP69913.
PaxDbiP69913.
PRIDEiP69913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75738; AAC75738; b2696.
BAA16558; BAA16558; BAA16558.
GeneIDi5551697.
947176.
KEGGiecj:JW2666.
eco:b2696.
PATRICi32120786. VBIEscCol129921_2785.

Organism-specific databases

EchoBASEiEB1416.
EcoGeneiEG11447. csrA.

Phylogenomic databases

eggNOGiCOG1551. LUCA.
HOGENOMiHOG000020767.
InParanoidiP69913.
KOiK03563.
OMAiIYARIQR.
OrthoDBiEOG6DC6PM.
PhylomeDBiP69913.

Enzyme and pathway databases

BioCyciEcoCyc:EG11447-MONOMER.
ECOL316407:JW2666-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69913.
PROiP69913.

Family and domain databases

HAMAPiMF_00167. CsrA.
InterProiIPR003751. CsrA.
[Graphical view]
PfamiPF02599. CsrA. 1 hit.
[Graphical view]
ProDomiPD009007. CsrA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR00202. csrA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties."
    Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.
    J. Bacteriol. 175:4744-4755(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Evidence for involvement of Escherichia coli genes pmbA, csrA and a previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F."
    Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T., Sekimizu K., Miki T.
    J. Mol. Biol. 256:483-502(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: KP4714.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The product of the pleiotropic Escherichia coli gene csrA modulates glycogen biosynthesis via effects on mRNA stability."
    Liu M.Y., Yang H., Romeo T.
    J. Bacteriol. 177:2663-2672(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "The RNA molecule CsrB binds to the global regulatory protein CsrA and antagonizes its activity in Escherichia coli."
    Liu M.Y., Gui G., Wei B., Preston J.F. III, Oakford L., Yuksel U., Giedroc D.P., Romeo T.
    J. Biol. Chem. 272:17502-17510(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSRB.
  8. "Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli."
    Wei B.L., Brun-Zinkernagel A.-M., Simecka J.W., Pruess B.M., Babitzke P., Romeo T.
    Mol. Microbiol. 40:245-256(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MOTILITY REGULATION.
  9. "Autoinducer 2 controls biofilm formation in Escherichia coli through a novel motility quorum-sensing regulator (MqsR, B3022)."
    Gonzalez Barrios A.F., Zuo R., Hashimoto Y., Yang L., Bentley W.E., Wood T.K.
    J. Bacteriol. 188:305-316(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290, K12 / DH5-alpha and K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "The RNA binding protein CsrA controls cyclic di-GMP metabolism by directly regulating the expression of GGDEF proteins."
    Jonas K., Edwards A.N., Simm R., Romeo T., Romling U., Melefors O.
    Mol. Microbiol. 70:236-257(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, FUNCTION IN DIGUANYLATE CYCLASE REGULATION, INDUCTION.
    Strain: K12.
  11. "Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress."
    Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D., Keck W., Ackermann M., Schirmer T., Jenal U.
    Mol. Microbiol. 72:1500-1516(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BIOFILM FORMATION, DISRUPTION PHENOTYPE.
    Strain: K12 / AB400.
  12. "Solution structure of the carbon storage regulator protein CsrA from Escherichia coli."
    Gutierrez P., Li Y., Osborne M.J., Pomerantseva E., Liu Q., Gehring K.
    J. Bacteriol. 187:3496-3501(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, RNA-BINDING, SUBUNIT.

Entry informationi

Entry nameiCSRA_ECOLI
AccessioniPrimary (citable) accession number: P69913
Secondary accession number(s): P31803
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: March 16, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.