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Entry version 129 (07 Apr 2021)
Sequence version 1 (01 Feb 1994)
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Protein

Translational regulator CsrA

Gene

csrA

Organism
Bacillus subtilis (strain 168)
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 translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Represses expression of flagellin (hag) in a post-transcriptional fashion. Specifically binds to 2 sites in the 5'-UTR of hag mRNA in a cooperative fashion; the second site overlaps the Shine-Dalgarno sequence and prevents 30S ribosomal subunit binding (PubMed:17555441). Mutation of either binding site abolishes CsrA regulation of hag expression (PubMed:17555441, PubMed:21895793). Repression is greater in the 1A96 than 168 genetic background and higher in minimal than rich medium (PubMed:17555441). Translation repression is antagonized by FliW (PubMed:21895793). Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagellin, which frees FliW to interact with CsrA and inhibits CsrA binding to mRNA. This derepresses flagellin translation and provides protein for flagellar assembly. Once the flagellar filament is completed cytoplasmic flagellin levels rise and CsrA translation repression of flagellin reinitiates (PubMed:21895793, PubMed:27516547). Overexpression leads to a dramatic reduction in motility, a significant reduction in flagellin synthesis and reduced flagella assembly (PubMed:21895793).3 Publications

<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

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 functionRepressor, RNA-binding
Biological processTranslation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU35370-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:
Translational 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:csrAUniRule annotation
Synonyms:sow1 Publication, yviG
Ordered Locus Names:BSU35370
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<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

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

Increased expression of flagellin (hag), 30% decrease in motility halo (PubMed:17555441). Suppresses the motility loss and flagellar assembly defect of an fliW deletion (PubMed:21895793). Suppresses the phenotypes associated with deletion of the intracellular flagella chaperone fliS (PubMed:23144244).3 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>Mutagenesisi6R → L or W in sow-2 and sow28; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW. 2 Publications1
Mutagenesisi7K → E in sow-12; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW. 2 Publications1
Mutagenesisi14I → M: Inhibits motility and flagellar filament assembly, still binds FliW. Binds 5'-UTR of hag mRNA, is not completed by FliW. 1 Publication1
Mutagenesisi25V → G in sow-20; suppresses the motility loss and flagellar assembly defect of an fliW deletion. 1 Publication1
Mutagenesisi32L → P in sow-10; suppresses the motility loss and flagellar assembly defect of an fliW deletion. 1 Publication1
Mutagenesisi33G → R in sow-11; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW. 2 Publications1
Mutagenesisi36A → T or V in sow-8 and sow-4; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW. 2 Publications1
Mutagenesisi46E → K in sow-15; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW. 2 Publications1
Mutagenesisi49L → S: Inhibits motility and flagellar filament assembly, reduced binding of FliW. 1 Publication1
Mutagenesisi55N → D: Inhibits motility and flagellar filament assembly, greatly reduced binding of FliW. Binds 5'-UTR of hag mRNA, is not completed by FliW. 1 Publication1
Mutagenesisi58A → V: Inhibits motility and flagellar filament assembly, reduced binding of FliW. 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_00001770491 – 74Translational regulator CsrAAdd BLAST74

Proteomic databases

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

More...
PaxDbi
P33911

PRoteomics IDEntifications database

More...
PRIDEi
P33911

<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

Part of the SigD-controlled yvyF-csrA operon and the SigA-controlled fliW-csrA operon (PubMed:17555441). Expressed from the SigA operon at low levels during log phase, with a 5-fold increase as the culture transitions to stationary phase, peaking 1 hour later.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%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 (PubMed:17555441). The beta-strands of each monomer intercalate to form a hydrophobic core while the alpha-helices form wings that extend away from the core (By similarity). Two molecules of FliW interact with 1 homodimer (PubMed:21895793, PubMed:27516547). mRNA and FliW bind to different sites on CsrA (PubMed:27516547).

By similarity1 Publication2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU35370

<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

174
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
P33911

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P33911

<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 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

Contacts FliW via its C-terminus (residues 49-58).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

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eggNOGi
COG1551, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P33911

Identification of Orthologs from Complete Genome Data

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OMAi
IHRKEVY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P33911

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.1680, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00167, CsrA, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003751, CsrA
IPR036107, CsrA_sf

The PANTHER Classification System

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PANTHERi
PTHR34984, PTHR34984, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02599, CsrA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF117130, SSF117130, 1 hit

TIGRFAMs; a protein family database

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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.

P33911-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLVLSRKINE AIQIGADIEV KVIAVEGDQV KLGIDAPKHI DIHRKEIYLT
60 70
IQEENNRAAA LSSDVISALS SQKK
Length:74
Mass (Da):8,136
Last modified:February 1, 1994 - 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:i10E82DA62D3174B5
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
M26948 Genomic DNA No translation available.
U56901 Genomic DNA Translation: AAC44950.1
AL009126 Genomic DNA Translation: CAB15554.1

Protein sequence database of the Protein Information Resource

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PIRi
H69608

NCBI Reference Sequences

More...
RefSeqi
NP_391417.1, NC_000964.3
WP_003219727.1, NZ_JNCM01000033.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB15554; CAB15554; BSU_35370

Database of genes from NCBI RefSeq genomes

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GeneIDi
936731

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU35370

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.3828

<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
M26948 Genomic DNA No translation available.
U56901 Genomic DNA Translation: AAC44950.1
AL009126 Genomic DNA Translation: CAB15554.1
PIRiH69608
RefSeqiNP_391417.1, NC_000964.3
WP_003219727.1, NZ_JNCM01000033.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T3ONMR-A1-74[»]
SMRiP33911
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU35370

Proteomic databases

PaxDbiP33911
PRIDEiP33911

Genome annotation databases

EnsemblBacteriaiCAB15554; CAB15554; BSU_35370
GeneIDi936731
KEGGibsu:BSU35370
PATRICifig|224308.179.peg.3828

Phylogenomic databases

eggNOGiCOG1551, Bacteria
InParanoidiP33911
OMAiIHRKEVY
PhylomeDBiP33911

Enzyme and pathway databases

BioCyciBSUB:BSU35370-MONOMER

Miscellaneous databases

EvolutionaryTraceiP33911

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_BACSU
<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: P33911
<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: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 7, 2021
This is version 129 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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