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Entry version 141 (13 Nov 2019)
Sequence version 2 (01 Nov 1997)
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Protein

UDP-2,3-diacylglucosamine hydrolase

Gene

lpxH

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

Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom (PubMed:12000770). Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (PubMed:12000770, PubMed:12000771). Is essential for E.coli growth (PubMed:12000771). Does not cleave the unacylated UDP-GlcNAc, the mono-acylated UDP-3-O-(R)-3-hydroxymyristoyl-GlcNAc, and CDP-diacylglycerol (PubMed:12000770).2 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>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

Mn2+UniRule annotation1 PublicationNote: Binds 2 Mn2+ ions per subunit in a binuclear metal center.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by a sulfonyl piperazine compound that shows antibacterial activity against E.coli; LpxH is the cellular target of this compound (PubMed:25733621). Inhibited by 0.01% (or more) Triton X-100 in vitro (PubMed:12000770).2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Assays with partially purified enzyme.1 Publication
  1. KM=61.7 µM for UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine1 Publication
  1. Vmax=17.2 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lipid IV(A) biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation2 Publications
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA), Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
  2. UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC), UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
  3. UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD), UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD), UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD), UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD)
  4. UDP-2,3-diacylglucosamine hydrolase (lpxH), UDP-2,3-diacylglucosamine hydrolase (lpxH), UDP-2,3-diacylglucosamine hydrolase (lpxH), UDP-2,3-diacylglucosamine hydrolase (lpxH)
  5. Lipid-A-disaccharide synthase (lpxB), Lipid-A-disaccharide synthase (lpxB), Lipid-A-disaccharide synthase (lpxB), Lipid-A-disaccharide synthase (lpxB), Lipid-A-disaccharide synthase (lpxB)
  6. Tetraacyldisaccharide 4'-kinase (lpxK), Tetraacyldisaccharide 4'-kinase (lpxK), Tetraacyldisaccharide 4'-kinase (lpxK), Tetraacyldisaccharide 4'-kinase (lpxK), Tetraacyldisaccharide 4'-kinase (lpxK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

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 bindingi8Manganese 1UniRule annotation1
Metal bindingi10Manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi41Manganese 1UniRule annotation1
Metal bindingi41Manganese 2UniRule annotation1
Metal bindingi79Manganese 2UniRule annotation1
Metal bindingi114Manganese 2; via tele nitrogenUniRule 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 sitei122SubstrateUniRule annotation1
Binding sitei160SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Binding sitei167SubstrateUniRule annotation1
Metal bindingi195Manganese 2; via pros nitrogenUniRule annotation1
Binding sitei195Substrate; via tele nitrogenUniRule annotation1
Metal bindingi197Manganese 1; via tele nitrogenUniRule 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

  • manganese ion binding Source: UniProtKB-UniRule
  • UDP-2,3-diacylglucosamine hydrolase activity Source: UniProtKB

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 functionHydrolase
Biological processLipid A biosynthesis, Lipid biosynthesis, Lipid metabolism
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG12666-MONOMER
ECOL316407:JW0513-MONOMER
MetaCyc:EG12666-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.1.54 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00359;UER00480

<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:
UDP-2,3-diacylglucosamine hydrolase1 PublicationUniRule annotation (EC:3.6.1.54UniRule annotation2 Publications)
Alternative name(s):
UDP-2,3-diacylglucosamine diphosphataseUniRule annotation
UDP-2,3-diacylglucosamine pyrophosphatase1 Publication
<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:lpxH1 PublicationUniRule annotation
Synonyms:ybbF
Ordered Locus Names:b0524, JW0513
<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

Cell inner membrane, Cell membrane, Cytoplasm, 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

An insertion mutation defective in lpxH is not viable and accumulates UDP-2,3-diacylglucosamine.1 Publication

<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_00002141081 – 240UDP-2,3-diacylglucosamine hydrolaseAdd BLAST240

Proteomic databases

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

More...
PaxDbi
P43341

PRoteomics IDEntifications database

More...
PRIDEi
P43341

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262817, 215 interactors

Database of interacting proteins

More...
DIPi
DIP-10125N

Protein interaction database and analysis system

More...
IntActi
P43341, 20 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0524

<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

1240
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

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SMRi
P43341

Database of comparative protein structure models

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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>Regioni79 – 80Substrate bindingUniRule annotation2

<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 LpxH family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105F10 Bacteria
COG2908 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000261930

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P43341

KEGG Orthology (KO)

More...
KOi
K03269

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P43341

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00575 LpxH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024654 Calcineurin-like_PHP_lpxH
IPR010138 UDP-diacylglucosamine_Hdrlase

The PANTHER Classification System

More...
PANTHERi
PTHR34990:SF1 PTHR34990:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12850 Metallophos_2, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01854 lipid_A_lpxH, 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.

P43341-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATLFIADLH LCVEEPAITA GFLRFLAGEA RKADALYILG DLFEAWIGDD
60 70 80 90 100
DPNPLHRKMA AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE
110 120 130 140 150
KVLELYGRRV LIMHGDTLCT DDAGYQAFRA KVHKPWLQTL FLALPLFVRK
160 170 180 190 200
RIAARMRANS KEANSSKSLA IMDVNQNAVV SAMEKHQVQW LIHGHTHRPA
210 220 230 240
VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
Length:240
Mass (Da):26,894
Last modified:November 1, 1997 - 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:i5004A2E471B7A7E9
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
AF311865 Genomic DNA Translation: AAG47820.1
U82664 Genomic DNA Translation: AAB40277.1
U00096 Genomic DNA Translation: AAC73626.1
AP009048 Genomic DNA Translation: BAE76301.1
M19657 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
C64784

NCBI Reference Sequences

More...
RefSeqi
NP_415057.1, NC_000913.3
WP_000212247.1, NZ_SSZK01000024.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73626; AAC73626; b0524
BAE76301; BAE76301; BAE76301

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
949053

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0513
eco:b0524

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1754

<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
AF311865 Genomic DNA Translation: AAG47820.1
U82664 Genomic DNA Translation: AAB40277.1
U00096 Genomic DNA Translation: AAC73626.1
AP009048 Genomic DNA Translation: BAE76301.1
M19657 Genomic DNA No translation available.
PIRiC64784
RefSeqiNP_415057.1, NC_000913.3
WP_000212247.1, NZ_SSZK01000024.1

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
5WLYX-ray2.00A1-240[»]
SMRiP43341
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262817, 215 interactors
DIPiDIP-10125N
IntActiP43341, 20 interactors
STRINGi511145.b0524

Proteomic databases

PaxDbiP43341
PRIDEiP43341

Genome annotation databases

EnsemblBacteriaiAAC73626; AAC73626; b0524
BAE76301; BAE76301; BAE76301
GeneIDi949053
KEGGiecj:JW0513
eco:b0524
PATRICifig|1411691.4.peg.1754

Organism-specific databases

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

More...
EchoBASEi
EB2532

Phylogenomic databases

eggNOGiENOG4105F10 Bacteria
COG2908 LUCA
HOGENOMiHOG000261930
InParanoidiP43341
KOiK03269
PhylomeDBiP43341

Enzyme and pathway databases

UniPathwayiUPA00359;UER00480
BioCyciEcoCyc:EG12666-MONOMER
ECOL316407:JW0513-MONOMER
MetaCyc:EG12666-MONOMER
BRENDAi3.6.1.54 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P43341

Family and domain databases

HAMAPiMF_00575 LpxH, 1 hit
InterProiView protein in InterPro
IPR024654 Calcineurin-like_PHP_lpxH
IPR010138 UDP-diacylglucosamine_Hdrlase
PANTHERiPTHR34990:SF1 PTHR34990:SF1, 1 hit
PfamiView protein in Pfam
PF12850 Metallophos_2, 1 hit
TIGRFAMsiTIGR01854 lipid_A_lpxH, 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 nameiLPXH_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: P43341
Secondary accession number(s): P77440, Q2MBQ5
<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, 1995
Last sequence update: November 1, 1997
Last modified: November 13, 2019
This is version 141 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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