Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 117 (07 Apr 2021)
Sequence version 1 (22 Nov 2005)
Previous versions | rss
Add a publicationFeedback
Protein

DNA-binding protein StpA

Gene

stpA

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 DNA-binding protein that acts in a fashion similar to H-NS protein upon overexpression, represses a number of genes including the cryptic blg operon, hns, papB and the proU locus (PubMed:8890170). A subset of H-NS/StpA-regulated genes also require Hha for repression; Hha and Cnu (YdgT) increases the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex (PubMed:23543115). Repression can be inhibited by dominant-negative mutants of StpA or H-NS (PubMed:8755860).3 Publications
(Microbial infection) Originally isolated as a suppressor of a splicing defect of the thymidylate synthase (td) gene from bacteriophage T4 (PubMed:1480493). Acts as an RNA chaperone, accelerating splicing of viral pre-mRNA. Binds preferentially to unstructured over structured RNA; does not have a detectable high-affinity RNA-binding site in the pre-mRNA. There do not seem to be any specific RNA targets in transcribed E.coli DNA (PubMed:17267410).2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi112 – 117By similarity6

<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 functionChaperone, DNA-binding, RNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11554-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:
DNA-binding protein StpA
Alternative name(s):
H-NS homolog StpA
<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:stpA1 Publication
Synonyms:hnsB
Ordered Locus Names:b2669, JW2644
<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

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

No visible phenotype in rich medium; double hns-stpA mutants grow slower and have reduced viable cell counts compared to single hns mutants in MC1029 and MC4100 backgrounds (PubMed:8890170). In 0.3M NaCl a double hns-stpA deletion up-regulates 583 and down-regulates 86 genes, 363 of which are thought to have been horizontally acquired; 131 are also up-regulated in a double cnu-hha deletion (PubMed:23543115).2 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>Mutagenesisi26L → P: Partial loss of repressor function when overexpressed in the absence of hns. 1 Publication1
Mutagenesisi65 – 134Missing : Partial loss of repressor function when overexpressed in the absence of hns. 1 PublicationAdd BLAST70
Mutagenesisi97Y → C: Partial loss of repressor function when overexpressed in the absence of hns. 1 Publication1
Mutagenesisi116P → S: Partial loss of repressor function when overexpressed in the absence of hns. 1 Publication1
Mutagenesisi126G → V: Higher RNA chaperone activity than wild-type, decreased ability to bind structured RNA. 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_00001685131 – 134DNA-binding protein StpAAdd BLAST134

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0ACG1

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

More...
PaxDbi
P0ACG1

PRoteomics IDEntifications database

More...
PRIDEi
P0ACG1

<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

Expressed at low levels at 37 degrees Celsius, barely detectable at 26 degrees Celsius; expression is repressed by hns and partially activated by lrp (PubMed:8890170).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

When overexpressed forms homodimers, can interact with the N-terminus (residues 1-64) of H-NS (PubMed:8755860). May interact with Hha and/or Cnu.

Curated1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262261, 8 interactors
851464, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-35951N

Protein interaction database and analysis system

More...
IntActi
P0ACG1, 24 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2669

<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

1134
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P0ACG1

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

More...
SMRi
P0ACG1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi42 – 45Poly-Glu4

<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

Both the N-terminus (residues 1-76) and the C-terminus (residues 90-134) have RNA chaperone activity for splicing of td, a bacteriophage T4 pre-mRNA (PubMed:17267410).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 histone-like protein H-NS family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2916, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_117503_0_0_6

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.287.1050, 1 hit
4.10.430.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027444, H-NS_C_dom
IPR037150, H-NS_C_dom_sf
IPR001801, Histone_HNS
IPR027454, Histone_HNS_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00816, Histone_HNS, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002096, HnS, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00528, HNS, 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.

P0ACG1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVMLQSLNN IRTLRAMARE FSIDVLEEML EKFRVVTKER REEEEQQQRE
60 70 80 90 100
LAERQEKIST WLELMKADGI NPEELLGNSS AAAPRAGKKR QPRPAKYKFT
110 120 130
DVNGETKTWT GQGRTPKPIA QALAEGKSLD DFLI
Length:134
Mass (Da):15,348
Last modified:November 22, 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:i5870BD95F144CE6A
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
X69210 Genomic DNA Translation: CAA49146.1
U07823 Genomic DNA Translation: AAA64940.1
U00096 Genomic DNA Translation: AAC75716.1
AP009048 Genomic DNA Translation: BAA16535.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JH0774

NCBI Reference Sequences

More...
RefSeqi
NP_417155.1, NC_000913.3
WP_000115383.1, NZ_STEB01000042.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75716; AAC75716; b2669
BAA16535; BAA16535; BAA16535

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57728672
947130

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2644
eco:b2669

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4072

<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
X69210 Genomic DNA Translation: CAA49146.1
U07823 Genomic DNA Translation: AAA64940.1
U00096 Genomic DNA Translation: AAC75716.1
AP009048 Genomic DNA Translation: BAA16535.1
PIRiJH0774
RefSeqiNP_417155.1, NC_000913.3
WP_000115383.1, NZ_STEB01000042.1

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
2LRXNMR-A90-134[»]
BMRBiP0ACG1
SMRiP0ACG1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262261, 8 interactors
851464, 2 interactors
DIPiDIP-35951N
IntActiP0ACG1, 24 interactors
STRINGi511145.b2669

Proteomic databases

jPOSTiP0ACG1
PaxDbiP0ACG1
PRIDEiP0ACG1

Genome annotation databases

EnsemblBacteriaiAAC75716; AAC75716; b2669
BAA16535; BAA16535; BAA16535
GeneIDi57728672
947130
KEGGiecj:JW2644
eco:b2669
PATRICifig|1411691.4.peg.4072

Organism-specific databases

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

More...
EchoBASEi
EB1515

Phylogenomic databases

eggNOGiCOG2916, Bacteria
HOGENOMiCLU_117503_0_0_6

Enzyme and pathway databases

BioCyciEcoCyc:EG11554-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0ACG1

Family and domain databases

Gene3Di1.10.287.1050, 1 hit
4.10.430.10, 1 hit
InterProiView protein in InterPro
IPR027444, H-NS_C_dom
IPR037150, H-NS_C_dom_sf
IPR001801, Histone_HNS
IPR027454, Histone_HNS_N
PfamiView protein in Pfam
PF00816, Histone_HNS, 1 hit
PIRSFiPIRSF002096, HnS, 1 hit
SMARTiView protein in SMART
SM00528, HNS, 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 nameiSTPA_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: P0ACG1
Secondary accession number(s): P30017
<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: November 22, 2005
Last sequence update: November 22, 2005
Last modified: April 7, 2021
This is version 117 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
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