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UniProtKB - O69078 (CSRA_PSEAE)

Protein

Translational regulator CsrA

Gene

csrA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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. 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. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s).UniRule annotation
Binds to mRNA to regulate gene activity at a post-transcriptional level (Probable). Represses expression of many toxic extracellular enzymes and compounds; decreases translation of lasI and rhlI (PubMed:11673439). Positively controls swarming motility and rhanolipid and lipase, possibly via expression of rhlA; activates transcription of the CsrA/RsmA antagonistic sRNA RsmZ (PubMed:15126453). Overexpression dramatically reduces extracellular protease, elastase (lasB) and staphyolytic (lasA) activities, decreases HCN production, decreases levels of autoinducers 3-oxo-C12-HSL (3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide) and C4-HSL (N-butanoylhomoserine lactone), and abolishes production of cytotoxic internal lectin PA-IL (lecA) (PubMed:11673439). Control of hcn expression is post-transcriptional (PubMed:11673439). Replaces endogenous gene(s) in E.coli and P.fluorescens (PubMed:16359708).3 Publications
Probably binds to and is sequestered by non-coding small RNA (sRNA) RsmZ; overexpression of rsmZ produces very similar phenotypes to deletion of rsmA, while rsmZ deletion has no phenotype (PubMed:15126453).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

  • mRNA 5'-UTR binding Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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		PAER208964:G1FZ6-921-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_and_taxonomy_section">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:
Translational regulator CsrAUniRule annotation
Alternative name(s):
Carbon storage regulatorUniRule annotation
Global translational regulatory protein RsmA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:csrAUniRule annotation
Synonyms:rsmA1 Publication
Ordered Locus Names:PA0905
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri208964 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002438 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Organism-specific databases

Pseudomonas genome database

More...PseudoCAPi		PA0905

<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

  • cytosol Source: GO_Central
View the complete GO annotation on QuickGO ...

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

Grows slightly more slowly; 30% reduction in staphylolytic activity, increased production of lectin PA-IL, blue-green pigment pyocyanine and HCN (PubMed:11673439). Increases levels of autoinducers 3-oxo-C12-HSL (3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide) and C4-HSL (N-butanoylhomoserine lactone) in early log phase which becomes nearly wild-type (3-oxo-C12-HSL) or 2-fold greater (C4-HSL) by late log phase (PubMed:11673439). Loss of swarming mobility and rhamnolipid production, loss of sRNA RsmZ expression, decreased lipase, increases synthesis of pyocyanine and HCN (PubMed:15126453). Loss of swarming mobility, overproduction of pyocyanine, reduction in lipase biosynthesis (PubMed:16359708).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi10E → A: Behaves like wild-type in swarming, pyocyanine production and lipase biosynthesis assays. 1 Publication1
Mutagenesisi44R → A: Does not complement deletion in swarming, pyocyanine production or lipase biosynthesis assays. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001770801 – 61Translational regulator CsrAAdd BLAST61

Proteomic databases

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

More...PaxDbi		O69078

PRoteomics IDEntifications database

More...PRIDEi		O69078

<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

Low levels of expression in early log phase, increases about 3-fold by stationary phase (at protein level) (PubMed:11673439).1 Publication

<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_section">'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_section">'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:16104018).UniRule annotation1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		208964.PA0905

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O69078

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

More...SMRi		O69078

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O69078

<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

<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		ENOG4105VM8 Bacteria
COG1551 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000020767

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O69078

KEGG Orthology (KO)

More...KOi		K03563

Identification of Orthologs from Complete Genome Data

More...OMAi		IHRKEVY

Database for complete collections of gene phylogenies

More...PhylomeDBi		O69078

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

ProDom; a protein domain database

More...ProDomi		View protein in ProDom or Entries sharing at least one domain
PD009007 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

O69078-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLILTRRVGE TLMVGDDVTV TVLGVKGNQV RIGVNAPKEV AVHREEIYQR 
        60 
IQKEKDQEPN H
Length:61
Mass (Da):6,909
Last modified:August 1, 1998 - 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:i3F5EDCD8AD28BB10
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF061757 Genomic DNA Translation: AAC16242.1
AE004091 Genomic DNA Translation: AAG04294.1

Protein sequence database of the Protein Information Resource

More...PIRi		D83531

NCBI Reference Sequences

More...RefSeqi		NP_249596.1, NC_002516.2
WP_003085981.1, NC_002516.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAG04294; AAG04294; PA0905

Database of genes from NCBI RefSeq genomes

More...GeneIDi		34383519
878352

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		pae:PA0905

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|208964.12.peg.940

<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
AF061757 Genomic DNA Translation: AAC16242.1
AE004091 Genomic DNA Translation: AAG04294.1
PIRiD83531
RefSeqiNP_249596.1, NC_002516.2
WP_003085981.1, NC_002516.2

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
1VPZX-ray2.05A/B1-61[»]
ProteinModelPortaliO69078
SMRiO69078
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0905

Proteomic databases

PaxDbiO69078
PRIDEiO69078

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		878352
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG04294; AAG04294; PA0905
GeneIDi34383519
878352
KEGGipae:PA0905
PATRICifig|208964.12.peg.940

Organism-specific databases

PseudoCAPiPA0905

Phylogenomic databases

eggNOGiENOG4105VM8 Bacteria
COG1551 LUCA
HOGENOMiHOG000020767
InParanoidiO69078
KOiK03563
OMAiIHRKEVY
PhylomeDBiO69078

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-921-MONOMER

Miscellaneous databases

EvolutionaryTraceiO69078

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
ProDomiView protein in ProDom or Entries sharing at least one domain
PD009007 CsrA, 1 hit
SUPFAMiSSF117130 SSF117130, 1 hit
TIGRFAMsiTIGR00202 csrA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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_PSEAE
<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: O69078
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: November 7, 2018
This is version 110 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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