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Entry version 118 (07 Apr 2021)
Sequence version 1 (06 Dec 2005)
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Protein

Periplasmic chaperone PpiD

Gene

ppiD

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

Chaperone that functions as a gatekeeper on the periplasmic side of the SecYEG translocon (PubMed:18439025, PubMed:20920237, PubMed:29097228). Facilitates the translocation of precursor proteins across SecYEG by interacting with the translocating substrate (PubMed:29097228). Also plays a role in the release of newly synthesized secreted proteins at the periplasmic exit site of the Sec translocon (PubMed:18439025, PubMed:20920237, PubMed:29097228). May be involved in the early periplasmic folding of many newly translocated proteins (PubMed:18439025, PubMed:20920237). Acts as a transient subunit of the Sec translocon that binds to the lateral gate of SecY and is detached by nascent membrane proteins but not by SecA (PubMed:24951590).4 Publications
Does not have peptidyl-prolyl isomerase (PPIase) activity. PPIase activity could not be generated by substitutions at the peptide binding site of the isolated parvulin-like domain.1 Publication
(Microbial infection) May play an important role in bacteriophage T4 infection and be involved in the penetration of the inner membrane by the bacteriophage injection machinery, resulting in a DNA-conducting channel to translocate the phage DNA into the interior of the cell.1 Publication

Miscellaneous

Overexpression restores viability of surA skp double deletion mutant but it does not completely compensate for the growth defect caused by the simultaneous lack of the SurA and Skp chaperones. Suppression of surA skp lethality does not require the parvulin domain but the membrane-localization of PpiD. In the absence of both SurA and Skp, overproduction of PpiD can, at least in part, counteract the defects in the biogenesis of OmpA and possibly of other OMPs.1 Publication

Caution

Was originally thought to be a peptidyl-prolyl isomerase (PPIase). It was shown later that even if PpiD shows sequence similarity to PPIases, it is in fact devoid of PPIase activity (PubMed:19866485).1 Publication1 Publication

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

GO - Biological processi

  • chaperone-mediated protein folding Source: EcoCyc

<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
Biological processStress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6242-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 chaperone PpiD1 Publication
Alternative name(s):
Periplasmic folding chaperoneCurated
<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:ppiD1 Publication
Synonyms:ybaU
Ordered Locus Names:b0441, JW0431
<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 15Cytoplasmic1 Publication1 PublicationAdd BLAST15
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei16 – 36HelicalSequence analysisAdd BLAST21
Topological domaini37 – 623Periplasmic1 Publication1 PublicationAdd BLAST587

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

Deletion of the gene retards the release of a translocating outer membrane protein into the periplasm (PubMed:18439025). Null mutation leads to the induction of the periplasmic stress response. Null mutants are hypersensitive to hydrophobic antibiotics such as novobiocin and to detergents such as SDS, and exhibit altered outer membrane proteins profile (PubMed:9670013). In contrast, another study shows that inactivation of the gene has no discernible effect on the levels of outer membrane proteins (PubMed:16267292). Lack of the gene confers increased temperature-sensitivity in a degP mutant (PubMed:20920237).4 Publications
(Microbial infection) Deletion of the gene leads to partial reduction in the plating efficiency of bacteriophage T4.1 Publication

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>Mutagenesisi312G → A or R: Cannot complement a surA null mutant or reduce the htrA-lacZ activity induced by periplasmic stresses. 1 Publication1
Mutagenesisi313G → A or R: Cannot complement a surA null mutant or reduce the htrA-lacZ activity induced by periplasmic stresses. 1 Publication1
Mutagenesisi347G → A: Can complement the growth defect of surA skp double deletion mutant. Has originally been reported to eliminate PPIase activity and to result in the loss of its reported surA complementing function. 2 Publications1
Mutagenesisi350I → A: Can complement the growth defect of surA skp double deletion mutant. Has originally been reported to eliminate PPIase activity and to result in the loss of its reported surA complementing function. 2 Publications1
Mutagenesisi350I → F: Cannot complement a surA null mutant or reduce the htrA-lacZ activity induced by periplasmic stresses. 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_00001934231 – 623Periplasmic chaperone PpiDAdd BLAST623

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0ADY1

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

More...
PaxDbi
P0ADY1

PRoteomics IDEntifications database

More...
PRIDEi
P0ADY1

<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

By heat shock via the sigma factor RpoH (PubMed:9670013). Member of the two-component system CpxA/CpxR regulon (PubMed:9670013).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

Interacts with the SecYEG translocon (PubMed:24951590, PubMed:29097228, PubMed:31699901). Binds to the lateral gate of SecY (PubMed:24951590, PubMed:31699901).

Forms a complex with YfgM (PubMed:21210718, PubMed:24855643, PubMed:31699901).

Also interacts with YidC (PubMed:31699901).

Interacts with peptide substrates and misfolded proteins (PubMed:18498364, PubMed:19866485). Has been isolated as a homodimer and homotrimer from inner membrane preparations (PubMed:16079137).

8 Publications

(Microbial infection) Interacts with the central spike complex of bacteriophage T4.

1 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

P0ADY1
With#Exp.IntAct
itself2EBI-562001,EBI-562001

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260732, 206 interactors

Database of interacting proteins

More...
DIPi
DIP-39902N

Protein interaction database and analysis system

More...
IntActi
P0ADY1, 8 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0441

<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

1623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P0ADY1

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

More...
SMRi
P0ADY1

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
P0ADY1

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini266 – 355PpiCPROSITE-ProRule annotationAdd BLAST90

<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

Consists of an N-terminal helix that anchors PpiD in the inner membrane, followed by three domains that face the periplasm. The first or the third domain are probably chaperone domains. The second domain is a parvulin-like domain, which is devoid of catalytic activity. It shows a parvulin fold and resembles most closely the inactive first parvulin domain of SurA, which is part of the chaperone unit of this protein and presumably involved in substrate recognition.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 PpiD chaperone family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0760, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_023843_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0ADY1

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0ADY1

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000297, PPIase_PpiC
IPR023058, PPIase_PpiC_CS
IPR027304, Trigger_fact/SurA_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13145, Rotamase_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF109998, SSF109998, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01096, PPIC_PPIASE_1, 1 hit
PS50198, PPIC_PPIASE_2, 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.

P0ADY1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMDSLRTAAN SLVLKIIFGI IIVSFILTGV SGYLIGGGNN YAAKVNDQEI
60 70 80 90 100
SRGQFENAFN SERNRMQQQL GDQYSELAAN EGYMKTLRQQ VLNRLIDEAL
110 120 130 140 150
LDQYARELKL GISDEQVKQA IFATPAFQVD GKFDNSRYNG ILNQMGMTAD
160 170 180 190 200
QYAQALRNQL TTQQLINGVA GTDFMLKGET DELAALVAQQ RVVREATIDV
210 220 230 240 250
NALAAKQPVT EQEIASYYEQ NKNNFMTPEQ FRVSYIKLDA ATMQQPVSDA
260 270 280 290 300
DIQSYYDQHQ DQFTQPQRTR YSIIQTKTED EAKAVLDELN KGGDFAALAK
310 320 330 340 350
EKSADIISAR NGGDMGWLED ATIPDELKNA GLKEKGQLSG VIKSSVGFLI
360 370 380 390 400
VRLDDIQPAK VKSLDEVRDD IAAKVKHEKA LDAYYALQQK VSDAASNDTE
410 420 430 440 450
SLAGAEQAAG VKATQTGWFS KDNLPEELNF KPVADAIFNG GLVGENGAPG
460 470 480 490 500
INSDIITVDG DRAFVLRISE HKPEAVKPLA DVQEQVKALV QHNKAEQQAK
510 520 530 540 550
VDAEKLLVDL KAGKGAEAMQ AAGLKFGEPK TLSRSGRDPI SQAAFALPLP
560 570 580 590 600
AKDKPSYGMA TDMQGNVVLL ALDEVKQGSM PEDQKKAMVQ GITQNNAQIV
610 620
FEALMSNLRK EAKIKIGDAL EQQ
Length:623
Mass (Da):68,150
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:i0F646F687114A387
GO

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
D82943 Genomic DNA Translation: BAA11645.1
U82664 Genomic DNA Translation: AAB40197.1
U00096 Genomic DNA Translation: AAC73544.1
AP009048 Genomic DNA Translation: BAE76221.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A64774

NCBI Reference Sequences

More...
RefSeqi
NP_414975.1, NC_000913.3
WP_000969372.1, NZ_SSZK01000009.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73544; AAC73544; b0441
BAE76221; BAE76221; BAE76221

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57731620
946056

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0431
eco:b0441

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1835

<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
D82943 Genomic DNA Translation: BAA11645.1
U82664 Genomic DNA Translation: AAB40197.1
U00096 Genomic DNA Translation: AAC73544.1
AP009048 Genomic DNA Translation: BAE76221.1
PIRiA64774
RefSeqiNP_414975.1, NC_000913.3
WP_000969372.1, NZ_SSZK01000009.1

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
2KGJNMR-A264-357[»]
BMRBiP0ADY1
SMRiP0ADY1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260732, 206 interactors
DIPiDIP-39902N
IntActiP0ADY1, 8 interactors
STRINGi511145.b0441

Proteomic databases

jPOSTiP0ADY1
PaxDbiP0ADY1
PRIDEiP0ADY1

Genome annotation databases

EnsemblBacteriaiAAC73544; AAC73544; b0441
BAE76221; BAE76221; BAE76221
GeneIDi57731620
946056
KEGGiecj:JW0431
eco:b0441
PATRICifig|1411691.4.peg.1835

Organism-specific databases

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

More...
EchoBASEi
EB3038

Phylogenomic databases

eggNOGiCOG0760, Bacteria
HOGENOMiCLU_023843_1_1_6
InParanoidiP0ADY1
PhylomeDBiP0ADY1

Enzyme and pathway databases

BioCyciEcoCyc:G6242-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ADY1

Protein Ontology

More...
PROi
PR:P0ADY1

Family and domain databases

InterProiView protein in InterPro
IPR000297, PPIase_PpiC
IPR023058, PPIase_PpiC_CS
IPR027304, Trigger_fact/SurA_dom_sf
PfamiView protein in Pfam
PF13145, Rotamase_2, 1 hit
SUPFAMiSSF109998, SSF109998, 1 hit
PROSITEiView protein in PROSITE
PS01096, PPIC_PPIASE_1, 1 hit
PS50198, PPIC_PPIASE_2, 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 nameiPPID_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: P0ADY1
Secondary accession number(s): P77241, Q2MBY5
<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: April 7, 2021
This is version 118 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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