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Entry version 104 (07 Oct 2020)
Sequence version 1 (06 Dec 2005)
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Protein

Periplasmic protein CpxP

Gene

cpxP

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

Acts as an auxiliary protein in the Cpx two-component envelope stress response system, helping modulate the Cpx response systems response to some inducers (PubMed:25207645, PubMed:16303867). Binds the periplasmic domain of sensor histidine kinase CpxA, inhibiting induction of the Cpx envelope stress response in the absence of inducer; overexpression decreases Cpx pathway activity (PubMed:16166523, PubMed:21317318). Some periplasmic stimulii (shown for P pili subunit PapE and probably 0.3 M NaCl) increase CpxP's susceptibility to DegP, leading to CpxP degradation, inducing the Cpx pathway (PubMed:16166523, PubMed:16303867). Aids in combating extracytoplasmic protein-mediated toxicity (PubMed:9473036, PubMed:16303867, PubMed:21239493). Overexpression leads to degradation by DegP of misfolded P pili subunits in the periplasm (tested using PapE) (PubMed:21239493). Inhibits autophosphorylation of CpxA in reconstituted liposomes by 50% but has no effect on phosphatase activity of CpxA (PubMed:17259177, PubMed:21239493). Has mild protein chaperone activity (PubMed:21317898, PubMed:21239493).8 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

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

Biological processStress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G7816-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:
Periplasmic protein CpxP1 Publication
Alternative name(s):
ORF_o1671 Publication
Periplasmic accessory protein CpxP
<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:cpxP1 Publication
Synonyms:yiiO
Ordered Locus Names:b4484, JW5558
<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

Periplasm

<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

Hypersensitive to alkaline pH (greater than pH 8.8) (PubMed:9473036). Increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867).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>Mutagenesisi55Q → P: No longer inhibits Cpx pathway, protein more susceptible to DegP. 2 Publications1
Mutagenesisi56R → Q: No longer interacts with CpxA. 1 Publication1
Mutagenesisi59M → T: No longer inhibits Cpx pathway, protein more susceptible to DegP. 1 Publication1
Mutagenesisi60R → Q: No longer inhibits Cpx pathway. 1 Publication1
Mutagenesisi61D → E or V: No longer inhibits Cpx pathway. 1 Publication1
Mutagenesisi103A → D or G: Decreased protein stability, significantly reduced degradation of PapE. 1 Publication1
Mutagenesisi107I → D: Decreased protein stability, significantly reduced degradation of PapE. 1 Publication1
Mutagenesisi107I → G or N: Decreased protein stability, wild-type degradation of PapE. 1 Publication1
Mutagenesisi108A → D: Decreased protein stability, significantly reduced degradation of PapE. 1 Publication1
Mutagenesisi108A → G: Decreased protein stability, wild-type degradation of PapE. 1 Publication1
Mutagenesisi108A → V: Decreased protein stability, significantly reduced degradation of PapE, retains most Cpx inhibition activity. 2 Publications1
Mutagenesisi128Q → H: No longer inhibits Cpx pathway in wild-type cells, protein more susceptible to DegP, in the absence of DegP protease partially inhibits Cpx. 2 Publications1

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<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_000002099222 – 166Periplasmic protein CpxPAdd BLAST145

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Degraded by DegP; some CpxP mutant proteins are more susceptible to the protease than others (PubMed:16166523). Degradation probably occurs when CpxP is associated with some misfolded proteins; overexpression of PapE leads to DegP-mediated degradation of CpxP and PapE, which requires the N-terminus of PapE. Overexpression of NlpE does not induce this degradation however (PubMed:16303867).2 Publications

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AE85

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

More...
PaxDbi
P0AE85

PRoteomics IDEntifications database

More...
PRIDEi
P0AE85

<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

Induced by envelope stress such as overexpression of misfolded periplasmic proteins (PubMed:9351822). Induced by alkaine pH (tested up to pH 8.4) (PubMed:9473036, PubMed:16166523). Induction is decreased in a degP deletion (PubMed:16166523). Transcription is stimulated by the Cpx two-component signal transduction pathway; sigma factor E (rpoE) is not involved (PubMed:9351822, PubMed:9473036, PubMed:10972835). Transcription induced by spheroplasting, which removes the periplasm and thus this protein; if the protein is anchored to the outer surface of the inner membrane induction does not occur (PubMed:10972835). Induced in persister cells (PubMed:16768798).5 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; it might alter shape slightly at pH 8.0 when Cpx is induced (PubMed:21317318, PubMed:21239493). Binds the periplasmic sensor domain of CpxA (PubMed:16166523, PubMed:21317318, PubMed:21239493, PubMed:25207645). Interaction with CpxA is not seen in vivo when cells are grown in 0.3 M NaCl, or if the misfolded P pili protein PapE is overexpressed (PubMed:25207645).

1 Publication3 Publications

<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

P0AE85
With#Exp.IntAct
itself2EBI-6413881,EBI-6413881

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262646, 127 interactors

Database of interacting proteins

More...
DIPi
DIP-47937N

Protein interaction database and analysis system

More...
IntActi
P0AE85, 4 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b4484

<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

1166
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

More...
SMRi
P0AE85

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
P0AE85

<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>Regioni55 – 61Important for protein stability, probably interacts with CpxA1 Publication7
Regioni151 – 166Not required for activation of CpxA or to induce degradation of misfolded P pili subunits1 PublicationAdd BLAST16

<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

A region in the N-terminus (residues 55-61) probably interacts with the periplasmic sensor domain of CpxA to inhibit its kinase activity and is also important for CpxP stability (PubMed:16166523). The homodimer has an elongated cradle shape; a hydrophobic cleft on the convex face may interact with periplasmic protein PapE (PubMed:21239493).2 Publications

<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 CpxP/Spy family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3678, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_124352_2_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AE85

KEGG Orthology (KO)

More...
KOi
K06006

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09916, CpxP_like, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012899, LTXXQ

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07813, LTXXQ, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF034445, CpxP_Spy, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE85-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRIVTAAVMA STLAVSSLSH AAEVGSGDNW HPGEELTQRS TQSHMFDGIS
60 70 80 90 100
LTEHQRQQMR DLMQQARHEQ PPVNVSELET MHRLVTAENF DENAVRAQAE
110 120 130 140 150
KMANEQIARQ VEMAKVRNQM YRLLTPEQQA VLNEKHQQRM EQLRDVTQWQ
160
KSSSLKLLSS SNSRSQ
Length:166
Mass (Da):18,965
Last modified:December 6, 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:iBD517D2D14D90209
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB03046 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L19201 Genomic DNA Translation: AAB03046.1 Different initiation.
U00096 Genomic DNA Translation: AAT48235.1
AP009048 Genomic DNA Translation: BAE77396.1

NCBI Reference Sequences

More...
RefSeqi
WP_001223800.1, NZ_STEB01000017.1
YP_026277.1, NC_000913.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAT48235; AAT48235; b4484
BAE77396; BAE77396; BAE77396

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2847688
48723770

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5558
eco:b4484

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2791

<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
L19201 Genomic DNA Translation: AAB03046.1 Different initiation.
U00096 Genomic DNA Translation: AAT48235.1
AP009048 Genomic DNA Translation: BAE77396.1
RefSeqiWP_001223800.1, NZ_STEB01000017.1
YP_026277.1, NC_000913.3

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
3ITFX-ray1.45A/B21-150[»]
3QZCX-ray2.85A/B40-151[»]
SMRiP0AE85
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262646, 127 interactors
DIPiDIP-47937N
IntActiP0AE85, 4 interactors
STRINGi511145.b4484

Proteomic databases

jPOSTiP0AE85
PaxDbiP0AE85
PRIDEiP0AE85

Genome annotation databases

EnsemblBacteriaiAAT48235; AAT48235; b4484
BAE77396; BAE77396; BAE77396
GeneIDi2847688
48723770
KEGGiecj:JW5558
eco:b4484
PATRICifig|1411691.4.peg.2791

Organism-specific databases

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

More...
EchoBASEi
EB1818

Phylogenomic databases

eggNOGiCOG3678, Bacteria
HOGENOMiCLU_124352_2_1_6
InParanoidiP0AE85
KOiK06006

Enzyme and pathway databases

BioCyciEcoCyc:G7816-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AE85

Protein Ontology

More...
PROi
PR:P0AE85

Family and domain databases

CDDicd09916, CpxP_like, 1 hit
InterProiView protein in InterPro
IPR012899, LTXXQ
PfamiView protein in Pfam
PF07813, LTXXQ, 1 hit
PIRSFiPIRSF034445, CpxP_Spy, 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 nameiCPXP_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: P0AE85
Secondary accession number(s): O65939, P32158, Q2M8L0
<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: December 6, 2005
Last sequence update: December 6, 2005
Last modified: October 7, 2020
This is version 104 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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