Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 112 (07 Oct 2020)
Sequence version 1 (22 Nov 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Lipid A biosynthesis lauroyltransferase

Gene

lpxL

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

Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo2-lipid IV(A) to form Kdo2-(lauroyl)-lipid IV(A). Has 10 fold selectivity for lauroyl-ACP over myristoyl-ACP. In vitro, can also catalyze a slow second acylation reaction leading to the formation of Kdo2-(dilauroyl)-lipid IV(A).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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

  1. KM=7 µM for lauroyl-ACP1 Publication
  2. KM=15 µM for Kdo2-lipid IV(A)1 Publication
  1. Vmax=95 µmol/min/mg enzyme toward lauroyl-ACP1 Publication
  2. Vmax=221 µmol/min/mg enzyme toward Kdo2-lipid IV(A)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: KDO(2)-lipid A biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A).UniRule annotation3 Publications
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 3-deoxy-D-manno-octulosonic acid transferase (waaA)
  2. 3-deoxy-D-manno-octulosonic acid transferase (waaA)
  3. Lipid A biosynthesis lauroyltransferase (lpxL), Lipid A biosynthesis lauroyltransferase (lpxL)
  4. Lipid A biosynthesis myristoyltransferase (lpxM), Lipid A biosynthesis myristoyltransferase (msbB)
This subpathway is part of the pathway KDO(2)-lipid 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 KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A), the pathway KDO(2)-lipid A biosynthesis and in Glycolipid biosynthesis.

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation3 Publications
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

<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

  • lauroyltransferase activity Source: UniProtKB-UniRule
  • transferase activity Source: EcoCyc

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 processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:LAUROYLACYLTRAN-MONOMER
MetaCyc:LAUROYLACYLTRAN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.B29, 2026

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

More...
UniPathwayi
UPA00030
UPA00360;UER00485

<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:
Lipid A biosynthesis lauroyltransferase1 PublicationUniRule annotation (EC:2.3.1.241UniRule annotation1 Publication)
Alternative name(s):
Kdo(2)-lipid IV(A) lauroyltransferaseUniRule annotation
<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:lpxL1 PublicationUniRule annotation
Synonyms:htrB1 Publication, waaM
Ordered Locus Names:b1054Imported, JW1041Imported
<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 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>Transmembranei17 – 37HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

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

Inactivation leads to bacterial death at temperatures above 33 degrees Celsius. Phenotype at nonpermissive temperatures includes an arrest of cell division followed by the formation of bulges or filaments.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>Mutagenesisi132H → A: Almost loss of activity. 1 Publication1
Mutagenesisi137E → A: Almost loss of activity. 1 Publication1
Mutagenesisi169R → A: 169-fold decrease in activity. 1 Publication1
Mutagenesisi200D → A: 14-fold decrease in activity. 1 Publication1
Mutagenesisi238P → A: Slight decrease in activity. 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_00002017741 – 306Lipid A biosynthesis lauroyltransferaseAdd BLAST306

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0ACV0

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

More...
PaxDbi
P0ACV0

PRoteomics IDEntifications database

More...
PRIDEi
P0ACV0

<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

Is expressed at all temperatures, but accumulation of htrB transcripts slightly declines with raising temperature. Thus, its expression is not induced by heat shock.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

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262842, 71 interactors

Protein interaction database and analysis system

More...
IntActi
P0ACV0, 9 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1054

<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

3D structure databases

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

More...
SMRi
P0ACV0

Database of comparative protein structure models

More...
ModBasei
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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi132 – 137HXXXXD motifUniRule annotation1 Publication6

<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 LpxL/LpxM/LpxP family.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1560, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_049421_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0ACV0

KEGG Orthology (KO)

More...
KOi
K02517

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0ACV0

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07984, LPLAT_LABLAT-like, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01942, Lipid_A_LpxL_LpxP, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004960, LipA_acyltrans
IPR011920, Lipid_A_LpxL_LpxP

The PANTHER Classification System

More...
PANTHERi
PTHR30606, PTHR30606, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03279, Lip_A_acyltrans, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF026649, MsbB, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02207, lipid_A_htrB, 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.

P0ACV0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTNLPKFSTA LLHPRYWLTW LGIGVLWLVV QLPYPVIYRL GCGLGKLALR
60 70 80 90 100
FMKRRAKIVH RNLELCFPEM SEQERRKMVV KNFESVGMGL METGMAWFWP
110 120 130 140 150
DRRIARWTEV IGMEHIRDVQ AQKRGILLVG IHFLTLELGA RQFGMQEPGI
160 170 180 190 200
GVYRPNDNPL IDWLQTWGRL RSNKSMLDRK DLKGMIKALK KGEVVWYAPD
210 220 230 240 250
HDYGPRSSVF VPLFAVEQAA TTTGTWMLAR MSGACLVPFV PRRKPDGKGY
260 270 280 290 300
QLIMLPPECS PPLDDAETTA AWMNKVVEKC IMMAPEQYMW LHRRFKTRPE

GVPSRY
Length:306
Mass (Da):35,407
Last modified:November 22, 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:iAEA70A5EB10653B5
GO

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
X61000 Genomic DNA Translation: CAA43317.1
U00096 Genomic DNA Translation: AAC74138.1
AP009048 Genomic DNA Translation: BAA35852.1
X59939 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
S16888

NCBI Reference Sequences

More...
RefSeqi
NP_415572.1, NC_000913.3
WP_000183364.1, NZ_STEB01000016.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74138; AAC74138; b1054
BAA35852; BAA35852; BAA35852

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
48135189
946216

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1041
eco:b1054

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.1095

<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
X61000 Genomic DNA Translation: CAA43317.1
U00096 Genomic DNA Translation: AAC74138.1
AP009048 Genomic DNA Translation: BAA35852.1
X59939 Genomic DNA No translation available.
PIRiS16888
RefSeqiNP_415572.1, NC_000913.3
WP_000183364.1, NZ_STEB01000016.1

3D structure databases

SMRiP0ACV0
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4262842, 71 interactors
IntActiP0ACV0, 9 interactors
STRINGi511145.b1054

Proteomic databases

jPOSTiP0ACV0
PaxDbiP0ACV0
PRIDEiP0ACV0

Genome annotation databases

EnsemblBacteriaiAAC74138; AAC74138; b1054
BAA35852; BAA35852; BAA35852
GeneIDi48135189
946216
KEGGiecj:JW1041
eco:b1054
PATRICifig|511145.12.peg.1095

Organism-specific databases

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

More...
EchoBASEi
EB0459

Phylogenomic databases

eggNOGiCOG1560, Bacteria
HOGENOMiCLU_049421_1_1_6
InParanoidiP0ACV0
KOiK02517
PhylomeDBiP0ACV0

Enzyme and pathway databases

UniPathwayiUPA00030
UPA00360;UER00485
BioCyciEcoCyc:LAUROYLACYLTRAN-MONOMER
MetaCyc:LAUROYLACYLTRAN-MONOMER
BRENDAi2.3.1.B29, 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0ACV0

Family and domain databases

CDDicd07984, LPLAT_LABLAT-like, 1 hit
HAMAPiMF_01942, Lipid_A_LpxL_LpxP, 1 hit
InterProiView protein in InterPro
IPR004960, LipA_acyltrans
IPR011920, Lipid_A_LpxL_LpxP
PANTHERiPTHR30606, PTHR30606, 1 hit
PfamiView protein in Pfam
PF03279, Lip_A_acyltrans, 1 hit
PIRSFiPIRSF026649, MsbB, 1 hit
TIGRFAMsiTIGR02207, lipid_A_htrB, 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 nameiLPXL_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: P0ACV0
Secondary accession number(s): P24187
<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: November 22, 2005
Last sequence update: November 22, 2005
Last modified: October 7, 2020
This is version 112 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

Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again