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UniProtKB - P0A850 (TIG_ECOLI)

Entry version 132 (18 Sep 2019)
Sequence version 1 (07 Jun 2005)
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Protein

Trigger factor

Gene

tig

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

Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates (PubMed:24812405). Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Isomerase, Rotamase
Biological processCell cycle, Cell division

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11003-MONOMER
ECOL316407:JW0426-MONOMER
MetaCyc:EG11003-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Trigger factor (EC:5.2.1.81 Publication)
Short name:
TF
Alternative name(s):
PPIase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tig
Ordered Locus Names:b0436, JW0426
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG11003 tig

<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

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at all at 43 degrees) and strain background.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44 – 46FRK → AAA: Decreases association with ribosomes. 1 Publication3
Mutagenesisi140M → E: Significantly decreases antiaggregation activity. 1 Publication1
Mutagenesisi374 – 387MASAY…EVIEF → AASAAEDPKEAIEA: Significantly decreased affinity for substrate PhoA, significantly decreases antiaggregation activity. 1 PublicationAdd BLAST14

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001793471 – 432Trigger factorAdd BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei45ADP-ribosylarginine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

(Microbial infection) ADP-ribosylated by the phage T4 protein ModB.1 Publication

Keywords - PTMi

ADP-ribosylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A850

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A850

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

More...PaxDbi		P0A850

PRoteomics IDEntifications database

More...PRIDEi		P0A850

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0A850

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF (PubMed:12452438); binding as a dimer has also been suggested (PubMed:12581648). Uncomplexed TF is in a monomer-dimer equilibrium with approximately two thirds of TF existing in a dimeric state; binding to substrate PhoA induces monomerization, 3 TF monomers bind somewhat independently to a single substrate molecule (PubMed:12452438, PubMed:24812405). TF and SRP can simultaneously bind to ribosomes; TF binding is abolished when SRP is bound to FtsY in the presence of a non-hydrolyzable GTP analog (PubMed:15148364). Contacts ribosomal proteins L23 and L29 (PubMed:12226666).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4259841, 557 interactors

Database of interacting proteins

More...DIPi		DIP-36226N

Protein interaction database and analysis system

More...IntActi		P0A850, 130 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0436

<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

1432
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		P0A850

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A850

<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_and_domains_section">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>Domaini161 – 246PPIase FKBP-typeAdd BLAST86

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>Regioni1 – 112Ribosome-binding1 PublicationAdd BLAST112
Regioni148 – 251Dispensable for chaperone activity, although its removal significantly decreases antiaggregation activity2 PublicationsAdd BLAST104

<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 3 domains; the N-terminus (residues 1-112) binds the ribosome, the middle domain (residues 150-246) has PPIase activity, while the discontinuous C-terminus (residues 113-149 and 247-432) binds substrate and has intrinsic chaperone activity on its own.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 FKBP-type PPIase family. Tig subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105DEA Bacteria
COG0544 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000218239

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A850

KEGG Orthology (KO)

More...KOi		K03545

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A850

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.3120.10, 1 hit
3.30.70.1050, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00303 Trigger_factor_Tig, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001179 PPIase_FKBP_dom
IPR005215 Trig_fac
IPR008880 Trigger_fac_C
IPR037041 Trigger_fac_C_sf
IPR008881 Trigger_fac_ribosome-bd_bac
IPR036611 Trigger_fac_ribosome-bd_sf
IPR027304 Trigger_fact/SurA_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR30560 PTHR30560, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00254 FKBP_C, 1 hit
PF05698 Trigger_C, 1 hit
PF05697 Trigger_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF003095 Trigger_factor, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF102735 SSF102735, 1 hit
SSF109998 SSF109998, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00115 tig, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50059 FKBP_PPIASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. 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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A850-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP 
        60         70         80         90        100
MNIVAQRYGA SVRQDVLGDL MSRNFIDAII KEKINPAGAP TYVPGEYKLG 
       110        120        130        140        150
EDFTYSVEFE VYPEVELQGL EAIEVEKPIV EVTDADVDGM LDTLRKQQAT 
       160        170        180        190        200
WKEKDGAVEA EDRVTIDFTG SVDGEEFEGG KASDFVLAMG QGRMIPGFED 
       210        220        230        240        250
GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFAINLKKV EERELPELTA 
       260        270        280        290        300
EFIKRFGVED GSVEGLRAEV RKNMERELKS AIRNRVKSQA IEGLVKANDI 
       310        320        330        340        350
DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL 
       360        370        380        390        400
LGEVIRTNEL KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN 
       410        420        430 
VALEEQAVEA VLAKAKVTEK ETTFNELMNQ QA
Length:432
Mass (Da):48,193
Last modified:June 7, 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:i42C3E3C335074164
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti118Q → E in AAA62791 (PubMed:2211496).Curated1
Sequence conflicti279 – 287KSAIRNRVK → RAPSVTALS in AAA62791 (PubMed:2211496).Curated9

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
M34066 Genomic DNA Translation: AAA62791.1
U00096 Genomic DNA Translation: AAC73539.1
AP009048 Genomic DNA Translation: BAE76216.1
U82664 Genomic DNA Translation: AAB40192.1
X17642 Genomic DNA Translation: CAA35634.1
J05534 Genomic DNA Translation: AAA23587.1

Protein sequence database of the Protein Information Resource

More...PIRi		D64773

NCBI Reference Sequences

More...RefSeqi		NP_414970.1, NC_000913.3
WP_001198386.1, NZ_STEB01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73539; AAC73539; b0436
BAE76216; BAE76216; BAE76216

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945081

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0426
eco:b0436

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1840

<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
M34066 Genomic DNA Translation: AAA62791.1
U00096 Genomic DNA Translation: AAC73539.1
AP009048 Genomic DNA Translation: BAE76216.1
U82664 Genomic DNA Translation: AAB40192.1
X17642 Genomic DNA Translation: CAA35634.1
J05534 Genomic DNA Translation: AAA23587.1
PIRiD64773
RefSeqiNP_414970.1, NC_000913.3
WP_001198386.1, NZ_STEB01000007.1

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
1L1PNMR-A148-249[»]
1OMSX-ray2.30A/B/C1-118[»]
1P9YX-ray2.15A/B1-118[»]
1W26X-ray2.70A/B1-432[»]
1W2BX-ray3.5051-144[»]
2MLXNMR-A1-432[»]
2MLYNMR-A1-432[»]
2MLZNMR-A1-432[»]
2VRHelectron microscopy19.00A1-432[»]
4URDelectron microscopy7.70A1-115[»]
5OWINMR-A/B1-432[»]
5OWJNMR-A/B1-432[»]
5ZR0NMR-A148-249[»]
6D6SNMR-A/B1-432[»]
SMRiP0A850
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4259841, 557 interactors
DIPiDIP-36226N
IntActiP0A850, 130 interactors
STRINGi511145.b0436

2D gel databases

SWISS-2DPAGEiP0A850

Proteomic databases

EPDiP0A850
jPOSTiP0A850
PaxDbiP0A850
PRIDEiP0A850

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73539; AAC73539; b0436
BAE76216; BAE76216; BAE76216
GeneIDi945081
KEGGiecj:JW0426
eco:b0436
PATRICifig|1411691.4.peg.1840

Organism-specific databases

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

More...EchoBASEi		EB0996
EcoGeneiEG11003 tig

Phylogenomic databases

eggNOGiENOG4105DEA Bacteria
COG0544 LUCA
HOGENOMiHOG000218239
InParanoidiP0A850
KOiK03545
PhylomeDBiP0A850

Enzyme and pathway databases

BioCyciEcoCyc:EG11003-MONOMER
ECOL316407:JW0426-MONOMER
MetaCyc:EG11003-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A850

Protein Ontology

More...PROi		PR:P0A850

Family and domain databases

Gene3Di1.10.3120.10, 1 hit
3.30.70.1050, 1 hit
HAMAPiMF_00303 Trigger_factor_Tig, 1 hit
InterProiView protein in InterPro
IPR001179 PPIase_FKBP_dom
IPR005215 Trig_fac
IPR008880 Trigger_fac_C
IPR037041 Trigger_fac_C_sf
IPR008881 Trigger_fac_ribosome-bd_bac
IPR036611 Trigger_fac_ribosome-bd_sf
IPR027304 Trigger_fact/SurA_dom_sf
PANTHERiPTHR30560 PTHR30560, 1 hit
PfamiView protein in Pfam
PF00254 FKBP_C, 1 hit
PF05698 Trigger_C, 1 hit
PF05697 Trigger_N, 1 hit
PIRSFiPIRSF003095 Trigger_factor, 1 hit
SUPFAMiSSF102735 SSF102735, 1 hit
SSF109998 SSF109998, 1 hit
TIGRFAMsiTIGR00115 tig, 1 hit
PROSITEiView protein in PROSITE
PS50059 FKBP_PPIASE, 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 nameiTIG_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: P0A850
Secondary accession number(s): P15299
, P22257, P77603, Q2MBZ0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: September 18, 2019
This is version 132 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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