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Entry version 121 (07 Oct 2020)
Sequence version 1 (04 Jan 2005)
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Protein

Carbon storage regulator

Gene

csrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability, initially identified for its effects on central carbon metabolism (PubMed:8393005). Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems (PubMed:21488981, PubMed:28924029). Binds to the 5'-UTR of mRNA to repress or activate translation; 2 binding sites on the homodimer can bridge 2 sites within target RNA (By similarity). Exerts reciprocal effects on enzymes of gluconeogenesis and glycogen biosynthesis versus those of glycolysis (PubMed:7493933, PubMed:16923806). Negatively effects glycogen biosynthesis, gluconeogenesis, alters cell size and surface properties (PubMed:8393005, PubMed:7751274, PubMed:7493933). Activates regulates expression of glycolysis genes (PubMed:7493933). Represses biofilm formation (PubMed:11741870). Regulates glycogen synthesis under both aerobic and anaerobic conditions; overexpression strongly inhibits glycogen accumulation (PubMed:8393005). Binds to 4 sites in its own promoter, including the Shine-Dalgarno sequence, repressing its own translation; mutating the binding-sites decreases repression (PubMed:21696456). Indirectly activates transcription from 1 of its 5 promoters, which is responsible for increased expression during stationary phase (PubMed:21696456). Binds to at least 720 transcripts in strain K12 / CF7789, many of which are also part of the stringent response, including relA, spoT and dksA; slightly represses RelA and slightly activates DskA translation (PubMed:21488981). Binds to and represses the ECF sigma factor rpoE promoter (PubMed:28924029). Accelerates the degradation of glgC gene transcripts; overexpression further decreases glgC transcripts (PubMed:7751274). Binds 2 sites in the glgC mRNA leader, 1 of which overlaps the Shine-Dalgarno sequence, preventing ribosome-binding and thus destabilizing the mRNA (PubMed:12067347). Acts to inhibit interaction between the CcdB (also known as LetD) protein and the A subunit of DNA gyrase (PubMed:8604133). Required to activate motility and flagellum biosynthesis through the post-transcriptional activation of flhDC expression by binding to and stabilizing the flhDC message (PubMed:11298291). Represses translation of iraD mRNA via translational coupling to an upstream open reading frame (PubMed:28851853). Binds to mRNA and reduces levels of probable diguanylate cyclases dgcT and dgcZ (PubMed:18713317).By similarity14 Publications
Binds to and is sequestered by non-coding small RNAs (sRNA) CsrB and CsrC which antagonize the activity of CsrA (PubMed:9211896, PubMed:12694612). The consensus RNA-binding site is CAGGA(U/A/C)G which is located in probable hairpin loops (PubMed:9211896). There are 18 sites in CsrB, which cooperatively binds about 18 copies of CsrA (PubMed:9211896, PubMed:12694612). CsrC has 9 sites, and cooperatively binds multiple copies of CsrA (PubMed:12694612). Indirectly activates expression of CsrB and CsrC, both dependently and independently of the BarA-UvrY two-component system (PubMed:12193630, PubMed:12694612). ppGpp activates transcription of CsrA-antagonistic small RNAs CsrB and CsrC, which downregulates CsrA's action on translation during the stringent response (PubMed:21488981).3 Publications

Miscellaneous

Identified as a multicopy suppressor of the slow growth phenotype of an rsgA (yjeQ) deletion mutant.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Repressor, RNA-binding
Biological processTranslation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11447-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Carbon storage regulatorCurated
Alternative name(s):
Translational dual regulator CsrAUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:csrA1 PublicationUniRule annotation
Synonyms:zfiA1 Publication
Ordered Locus Names:b2696, JW2666
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Essential, it cannot be deleted when cells grow on LB but cells will grow with pyruvate as the sole carbon source; if glycogen synthesis is impaired then cells become viable (PubMed:19103924). Most deletion experiments use an allele which has a kanamycin-resistance cassette inserted after amino acid 50, which retains about 10% residual activity (PubMed:8393005, PubMed:19103924). Increased levels of glgC transcripts during both exponential and stationary phases (PubMed:7751274). Decreased levels of enzymes involved in glycolysis (PubMed:7493933). Increased biofilm formation (PubMed:11741870). Decreased expression of it antagonistic small RNAs CsrB and CsrC (PubMed:12694612). Allows basal levels of poly-GlcNAc synthesis and biofilm formation; this disrupted strain serves as a model system for biofilm formation (PubMed:19460094). Increased expression of RelA, about 1.5-fold increase in (p)ppGpp levels (PubMed:21488981). Increased levels of ECF sigma factor E (rpoE) (PubMed:28924029).9 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2L → A: Loss of in vivo repression and activation, 73-fold decreased affinity for RNA, about 75% wild-type protein levels. 1 Publication1
Mutagenesisi3I → A: 80% loss of in vivo repression and activation, about 20% wild-type protein levels. 1 Publication1
Mutagenesisi4L → A: 90% loss of in vivo repression and activation, 60-fold decreased affinity for RNA, about 60% wild-type protein levels. 1 Publication1
Mutagenesisi6R → A: Nearly complete loss of in vivo repression and activation, 30-fold decreased affinity for RNA, about 175% wild-type protein levels. 1 Publication1
Mutagenesisi7R → A: 70% loss of in vivo repression and activation, 12-fold decreased affinity for RNA, about 125% wild-type protein levels. 1 Publication1
Mutagenesisi19T → A: Increased repression and activation in vivo, about 75% wild-type protein levels. 1 Publication1
Mutagenesisi35N → A: Increased repression and activation in vivo, about 75% wild-type protein levels. 1 Publication1
Mutagenesisi40V → A: 90% loss of in vivo repression and activation, 67-fold decreased affinity for RNA, about 75% wild-type protein levels. 1 Publication1
Mutagenesisi42V → A: Loss of in vivo repression and activation, 135-fold decreased affinity for RNA, about 40% wild-type protein levels. 1 Publication1
Mutagenesisi44R → A: Loss of in vivo repression and activation, 150-fold decreased affinity for RNA, >500% wild-type protein levels. 1 Publication1
Mutagenesisi47I → A: 90% loss of in vivo repression and activation, 67-fold decreased affinity for RNA, about 150% wild-type protein levels. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001770611 – 61Carbon storage regulatorAdd BLAST61

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P69913

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P69913

PRoteomics IDEntifications database

More...
PRIDEi
P69913

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Activated by MqsR (PubMed:16352847, PubMed:18713317). Activated by DksA and (p)ppGpp, under partial control of RpoS, the sigma stress factor (at protein level) (PubMed:21488981). Binds to 4 sites in its own mRNA and represses translation (PubMed:21696456). Expressed from 5 promoters; P2 and P5 depend on housekeeping sigma factor 70 (rpoD) while P1 and P3 2 depend on RpoS; indirect activation of P3 leads to increased transcription during the log to stationary phase shift (PubMed:21696456).4 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; the beta-strands of each monomer intercalate to form a hydrophobic core while the alpha-helices form wings that extend away from the core (PubMed:15866937, ECO:0000255|HAMAP-Rule:MF_00167).

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259421, 231 interactors
851508, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-47836N

Protein interaction database and analysis system

More...
IntActi
P69913, 10 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2696

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

161
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P69913

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P69913

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 7Region 1, important for regulation and mRNA-binding1 Publication6
Regioni40 – 47Region 2, important for regulation and mRNA-binding1 Publication8

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Two regions important for regulation and RNA-binding are found in the N-terminus (residues 2-7) and middle (residues 40-47). Both are part of the intercalated beta-strands that form the hydrophobic core of the protein; region 1 from one monomer contacts region 2 of the other. The homodimer has 2 distinct RNA-binding regions on opposite, solvent-exposed surface of the protein.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the CsrA/RsmA family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1551, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_164837_2_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P69913

KEGG Orthology (KO)

More...
KOi
K03563

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P69913

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.1680, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00167, CsrA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003751, CsrA
IPR036107, CsrA_sf

The PANTHER Classification System

More...
PANTHERi
PTHR34984, PTHR34984, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02599, CsrA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF117130, SSF117130, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00202, csrA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i16308FC572670E1C
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
B40608

NCBI Reference Sequences

More...
RefSeqi
NP_417176.1, NC_000913.3
WP_000906486.1, NZ_STEB01000027.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75738; AAC75738; b2696
BAA16558; BAA16558; BAA16558

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9127731
947176

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2666
eco:b2696

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4048

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_STEB01000027.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y00NMR-A/B1-61[»]
5Z38X-ray2.29E/G/I/K1-44[»]
F/H/J/L1-61[»]
SMRiP69913
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259421, 231 interactors
851508, 4 interactors
DIPiDIP-47836N
IntActiP69913, 10 interactors
STRINGi511145.b2696

Proteomic databases

jPOSTiP69913
PaxDbiP69913
PRIDEiP69913

Genome annotation databases

EnsemblBacteriaiAAC75738; AAC75738; b2696
BAA16558; BAA16558; BAA16558
GeneIDi9127731
947176
KEGGiecj:JW2666
eco:b2696
PATRICifig|1411691.4.peg.4048

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1416

Phylogenomic databases

eggNOGiCOG1551, Bacteria
HOGENOMiCLU_164837_2_1_6
InParanoidiP69913
KOiK03563
PhylomeDBiP69913

Enzyme and pathway databases

BioCyciEcoCyc:EG11447-MONOMER

Miscellaneous databases

EvolutionaryTraceiP69913

Protein Ontology

More...
PROi
PR:P69913

Family and domain databases

Gene3Di3.30.70.1680, 1 hit
HAMAPiMF_00167, CsrA, 1 hit
InterProiView protein in InterPro
IPR003751, CsrA
IPR036107, CsrA_sf
PANTHERiPTHR34984, PTHR34984, 1 hit
PfamiView protein in Pfam
PF02599, CsrA, 1 hit
SUPFAMiSSF117130, SSF117130, 1 hit
TIGRFAMsiTIGR00202, csrA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCSRA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P69913
Secondary accession number(s): P31803
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: October 7, 2020
This is version 121 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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