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Entry version 172 (13 Nov 2019)
Sequence version 2 (29 Aug 2003)
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Protein

tRNA N6-adenosine threonylcarbamoyltransferase

Gene

tsaD

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

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. May also be involved in the metabolism of glycated proteins, but does not show sialoglycoprotease activity against glycophorin A.3 Publications

Miscellaneous

TsaBCDE are necessary and sufficient for tRNA(NNU) t6A37 threonylcarbamoyladenosine modification in vitro in E.coli.1 Publication

Caution

Was proposed to be a ligase for bicarbonate and threonine (PubMed:21285948): in the first step, TsaD would catalyze transfer of a gamma-phosphate group from ATP to bicarbonate, yielding carboxyphosphate and ADP; carboxyphosphate would then react with the threonine amine, producing N-carbamoylthreonine and phosphate. However, the protein ortholog in B.subtilis was shown to be involved in another step of t6A37 biosynthesis, i.e. the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB (PubMed:23072323). The protein ortholog in yeast (QRI7) was also shown to catalyze this step, and does not require the presence of additional proteins (PubMed:23620299).1 Publication
The well-known t6A modification appears to be a hydrolyzed artifact of natural cyclic t6A (ct6A) that occurs during the preparation and handling of tRNA in E.coli and many other species (PubMed:23242255). In these species, the t6A modification is processed further by dehydration into ct6A, a reaction catalyzed by TcdA.Curated

<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>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi111IronUniRule annotation1
Metal bindingi115IronUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei167SubstrateUniRule annotation1
Binding sitei180Substrate; via amide nitrogenUniRule annotation1
Binding sitei272SubstrateUniRule annotation1
Metal bindingi300IronUniRule annotation1

<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 functionAcyltransferase, Transferase
Biological processtRNA processing
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11171-MONOMER
ECOL316407:JW3036-MONOMER
MetaCyc:EG11171-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.6.99.4 2026

<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:
tRNA N6-adenosine threonylcarbamoyltransferaseUniRule annotation (EC:2.3.1.234UniRule annotation1 Publication)
Alternative name(s):
N6-L-threonylcarbamoyladenine synthaseUniRule annotation
Short name:
t(6)A synthaseUniRule annotation
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaDUniRule annotation
tRNA threonylcarbamoyladenosine biosynthesis protein TsaDUniRule annotation
<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:tsaDUniRule annotation
Synonyms:gcp, ygjD
Ordered Locus Names:b3064, JW3036
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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

<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

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

Appears essential for growth, since no null mutants can be obtained. Conditional depletion of this gene prevents t6A37 modification, and leads to pleiotropic phenotypes including increased or reduced cell size, unusual distribution of DNA around the cell periphery, nucleoid loss, and membrane/cell envelope defects. These phenotypes could be indirect effects of severe translation defects. The TsaD depletion phenotype is suppressed by overexpressing the response regulator RstA.4 Publications

<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_00000969621 – 337tRNA N6-adenosine threonylcarbamoyltransferaseAdd BLAST337

<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

Can be proteolytically processed in vitro by TsaB.1 Publication

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P05852

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

More...
PaxDbi
P05852

PRoteomics IDEntifications database

More...
PRIDEi
P05852

<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.

Interacts with TsaB; may form a heterodimer with TsaB.

Also interacts with TsaC.

4 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

WithEntry#Exp.IntActNotes
P762568EBI-561994,EBI-560669

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261402, 87 interactors
851894, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1094 YgjD-YeaZ-YjeE complex

Database of interacting proteins

More...
DIPi
DIP-9749N

Protein interaction database and analysis system

More...
IntActi
P05852, 14 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3064

<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

1337
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
P05852

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

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>Regioni134 – 138Substrate bindingUniRule annotation5

<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 KAE1 / TsaD family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CPM Bacteria
COG0533 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000109568

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05852

KEGG Orthology (KO)

More...
KOi
K01409

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P05852

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01445 TsaD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000905 Gcp-like_dom
IPR017861 KAE1/TsaD
IPR017860 Peptidase_M22_CS
IPR022450 TsaD

The PANTHER Classification System

More...
PANTHERi
PTHR11735 PTHR11735, 1 hit
PTHR11735:SF6 PTHR11735:SF6, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00814 Peptidase_M22, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00789 OSIALOPTASE

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00329 gcp_kae1, 1 hit
TIGR03723 T6A_TsaD_YgjD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01016 GLYCOPROTEASE, 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.

P05852-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVLGIETSC DETGIAIYDD EKGLLANQLY SQVKLHADYG GVVPELASRD
60 70 80 90 100
HVRKTVPLIQ AALKESGLTA KDIDAVAYTA GPGLVGALLV GATVGRSLAF
110 120 130 140 150
AWDVPAIPVH HMEGHLLAPM LEDNPPEFPF VALLVSGGHT QLISVTGIGQ
160 170 180 190 200
YELLGESIDD AAGEAFDKTA KLLGLDYPGG PLLSKMAAQG TAGRFVFPRP
210 220 230 240 250
MTDRPGLDFS FSGLKTFAAN TIRDNGTDDQ TRADIARAFE DAVVDTLMIK
260 270 280 290 300
CKRALDQTGF KRLVMAGGVS ANRTLRAKLA EMMKKRRGEV FYARPEFCTD
310 320 330
NGAMIAYAGM VRFKAGATAD LGVSVRPRWP LAELPAA
Length:337
Mass (Da):36,008
Last modified:August 29, 2003 - v2
<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:iAD676E3B635EC637
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 conflicti136S → C in AAA72575 (PubMed:3297921).Curated1

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
M16194 Genomic DNA Translation: AAA72575.1
U28379 Genomic DNA Translation: AAA89144.1
U00096 Genomic DNA Translation: AAC76100.1
AP009048 Genomic DNA Translation: BAE77115.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F65094 QQECR6

NCBI Reference Sequences

More...
RefSeqi
NP_417536.1, NC_000913.3
WP_001264352.1, NZ_STEB01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76100; AAC76100; b3064
BAE77115; BAE77115; BAE77115

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947578

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3036
eco:b3064

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3666

<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
M16194 Genomic DNA Translation: AAA72575.1
U28379 Genomic DNA Translation: AAA89144.1
U00096 Genomic DNA Translation: AAC76100.1
AP009048 Genomic DNA Translation: BAE77115.1
PIRiF65094 QQECR6
RefSeqiNP_417536.1, NC_000913.3
WP_001264352.1, NZ_STEB01000001.1

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
4WQ4X-ray2.33A/B1-337[»]
4WQ5X-ray2.33A/B1-337[»]
4YDUX-ray2.33A/B1-337[»]
SMRiP05852
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261402, 87 interactors
851894, 3 interactors
ComplexPortaliCPX-1094 YgjD-YeaZ-YjeE complex
DIPiDIP-9749N
IntActiP05852, 14 interactors
STRINGi511145.b3064

Proteomic databases

EPDiP05852
PaxDbiP05852
PRIDEiP05852

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
947578

Genome annotation databases

EnsemblBacteriaiAAC76100; AAC76100; b3064
BAE77115; BAE77115; BAE77115
GeneIDi947578
KEGGiecj:JW3036
eco:b3064
PATRICifig|1411691.4.peg.3666

Organism-specific databases

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

More...
EchoBASEi
EB1158

Phylogenomic databases

eggNOGiENOG4105CPM Bacteria
COG0533 LUCA
HOGENOMiHOG000109568
InParanoidiP05852
KOiK01409
PhylomeDBiP05852

Enzyme and pathway databases

BioCyciEcoCyc:EG11171-MONOMER
ECOL316407:JW3036-MONOMER
MetaCyc:EG11171-MONOMER
BRENDAi2.6.99.4 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P05852

Family and domain databases

HAMAPiMF_01445 TsaD, 1 hit
InterProiView protein in InterPro
IPR000905 Gcp-like_dom
IPR017861 KAE1/TsaD
IPR017860 Peptidase_M22_CS
IPR022450 TsaD
PANTHERiPTHR11735 PTHR11735, 1 hit
PTHR11735:SF6 PTHR11735:SF6, 1 hit
PfamiView protein in Pfam
PF00814 Peptidase_M22, 1 hit
PRINTSiPR00789 OSIALOPTASE
TIGRFAMsiTIGR00329 gcp_kae1, 1 hit
TIGR03723 T6A_TsaD_YgjD, 1 hit
PROSITEiView protein in PROSITE
PS01016 GLYCOPROTEASE, 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 nameiTSAD_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: P05852
Secondary accession number(s): Q2M9E1
<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: November 1, 1988
Last sequence update: August 29, 2003
Last modified: November 13, 2019
This is version 172 of the entry and version 2 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, Reference proteome

Documents

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