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Entry version 176 (25 May 2022)
Sequence version 2 (23 Jan 2007)
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Protein

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

Gene

lpxD

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 N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3-hydroxytetradecanoyl-ACP over (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2' positions.

2 Publications

Caution

Was originally thought to be involved in transcription.Curated

<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 <a href="http://www.uniprot.org/help/function%5Fsection">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 divalent cations such as Ca2+ and Mg2+.1 Publication

<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

kcat is 23 sec(-1).
  1. KM=2.5 µM for UDP-3-O-((3R)-hydroxytetradecanoyl)-alpha-D-glucosamine1 Publication
  2. KM=3.2 µM for (3R)-3-hydroxytetradecanoyl-ACP1 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: lipid IV(A) biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine. 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%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei239Proton acceptor1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei290Involved in determining the hydroxyacyl-ACP selectivity1

<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

  • lipid A biosynthetic process Source: EcoliWiki
  • response to antibiotic Source: UniProtKB-KW

<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 processAntibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:UDPHYDROXYMYRGLUCOSAMNACETYLTRANS-MONO

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.191, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P21645

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

More...
UniPathwayi
UPA00359;UER00479

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001884

<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:
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC:2.3.1.1913 Publications)
Short name:
UDP-3-O-(3-OHC14)-GlcN N-acyltransferase
Alternative name(s):
Protein FirA
Rifampicin resistance protein
UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase
<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:lpxD
Synonyms:firA, omsA
Ordered Locus Names:b0179, JW0174
<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

<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

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>Mutagenesisi41F → A: 30-fold decrease in affinity for UDP-3-O-((3R)-hydroxytetradecanoyl)-GlcN and 5-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi165Q → R in firA200; confers temperature sensitivity and reverses the rifampicin resistance of rpoB mutants. 1 Publication1
Mutagenesisi172I → F in firA201; confers temperature sensitivity. 1
Mutagenesisi228G → D in firA200 and firA201; confers temperature sensitivity. 1 Publication1
Mutagenesisi239H → A: 1000-fold reduction in catalytic activity with very little effect on substrate affinity. 1 Publication1
Mutagenesisi252G → S in firA200 and firA201; confers temperature sensitivity. 1 Publication1
Mutagenesisi271S → N in omsA; confers temperature sensitivity. 1 Publication1
Mutagenesisi276H → A: 30-fold reduction in catalytic activity. 1 Publication1
Mutagenesisi290M → A: Change in the acyl donor selectivity, showing a preference for 3-hydroxypalmitoyl-ACP over 3-hydroxytetradecanoyl-ACP as substrate. Produces a lipid A with longer acyl chains. 1 Publication1
Mutagenesisi292M → A: No change in the acyl donor selectivity. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000596692 – 341UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferaseAdd BLAST340

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P21645

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

More...
PaxDbi
P21645

PRoteomics IDEntifications database

More...
PRIDEi
P21645

<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

Homotrimer.

2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259589, 448 interactors

Database of interacting proteins

More...
DIPi
DIP-10124N

Protein interaction database and analysis system

More...
IntActi
P21645, 56 interactors

STRING: functional protein association networks

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STRINGi
511145.b0179

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P21645

<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

1341
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P21645

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

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SMRi
P21645

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21645

<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

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1044, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_049865_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P21645

Identification of Orthologs from Complete Genome Data

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OMAi
QIQIAHN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P21645

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03352, LbH_LpxD, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00523, LpxD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001451, Hexapep
IPR018357, Hexapep_transf_CS
IPR007691, LpxD
IPR011004, Trimer_LpxA-like_sf
IPR020573, UDP_GlcNAc_AcTrfase_non-rep

The PANTHER Classification System

More...
PANTHERi
PTHR43378, PTHR43378, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00132, Hexapep, 3 hits
PF04613, LpxD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51161, SSF51161, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01853, lipid_A_lpxD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00101, HEXAPEP_TRANSFERASES, 4 hits

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P21645-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSIRLADLA QQLDAELHGD GDIVITGVAS MQSAQTGHIT FMVNPKYREH
60 70 80 90 100
LGLCQASAVV MTQDDLPFAK SAALVVKNPY LTYARMAQIL DTTPQPAQNI
110 120 130 140 150
APSAVIDATA KLGNNVSIGA NAVIESGVEL GDNVIIGAGC FVGKNSKIGA
160 170 180 190 200
GSRLWANVTI YHEIQIGQNC LIQSGTVVGA DGFGYANDRG NWVKIPQIGR
210 220 230 240 250
VIIGDRVEIG ACTTIDRGAL DDTIIGNGVI IDNQCQIAHN VVIGDNTAVA
260 270 280 290 300
GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV
310 320 330 340
YSSGIPLQPN KVWRKTAALV MNIDDMSKRL KSLERKVNQQ D
Length:341
Mass (Da):36,038
Last modified:January 23, 2007 - 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:iB0ADFED5B17C649D
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
X54797 Genomic DNA Translation: CAA38568.1
U70214 Genomic DNA Translation: AAB08608.1
U00096 Genomic DNA Translation: AAC73290.1
AP009048 Genomic DNA Translation: BAA77854.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S13729

NCBI Reference Sequences

More...
RefSeqi
NP_414721.1, NC_000913.3
WP_001139279.1, NZ_STEB01000032.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73290; AAC73290; b0179
BAA77854; BAA77854; BAA77854

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
66671533
944882

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0174
eco:b0179

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2100

<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
X54797 Genomic DNA Translation: CAA38568.1
U70214 Genomic DNA Translation: AAB08608.1
U00096 Genomic DNA Translation: AAC73290.1
AP009048 Genomic DNA Translation: BAA77854.1
PIRiS13729
RefSeqiNP_414721.1, NC_000913.3
WP_001139279.1, NZ_STEB01000032.1

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
3EH0X-ray2.60A/B/C1-341[»]
4IHFX-ray2.10A/B/C/D/E/F3-341[»]
4IHGX-ray2.89A/B/C/D/E/F3-341[»]
4IHHX-ray2.13A/B/C/D/E/F3-341[»]
6P83X-ray1.70A/B/C3-341[»]
6P84X-ray1.70A/B/C3-341[»]
6P85X-ray1.90A/B/C3-341[»]
6P86X-ray1.80A/B/C3-341[»]
6P87X-ray1.90A/B/C3-341[»]
6P88X-ray1.70A/B/C3-341[»]
6P89X-ray1.40A/B/C3-341[»]
6P8AX-ray1.80A/B/C3-341[»]
6P8BX-ray2.00A/B/C3-341[»]
AlphaFoldDBiP21645
SMRiP21645
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259589, 448 interactors
DIPiDIP-10124N
IntActiP21645, 56 interactors
STRINGi511145.b0179

Chemistry databases

BindingDBiP21645
SwissLipidsiSLP:000001884

Proteomic databases

jPOSTiP21645
PaxDbiP21645
PRIDEiP21645

Genome annotation databases

EnsemblBacteriaiAAC73290; AAC73290; b0179
BAA77854; BAA77854; BAA77854
GeneIDi66671533
944882
KEGGiecj:JW0174
eco:b0179
PATRICifig|1411691.4.peg.2100

Organism-specific databases

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

More...
EchoBASEi
EB0312

Phylogenomic databases

eggNOGiCOG1044, Bacteria
HOGENOMiCLU_049865_0_1_6
InParanoidiP21645
OMAiQIQIAHN
PhylomeDBiP21645

Enzyme and pathway databases

UniPathwayiUPA00359;UER00479
BioCyciEcoCyc:UDPHYDROXYMYRGLUCOSAMNACETYLTRANS-MONO
BRENDAi2.3.1.191, 2026
SABIO-RKiP21645

Miscellaneous databases

EvolutionaryTraceiP21645

Protein Ontology

More...
PROi
PR:P21645

Family and domain databases

CDDicd03352, LbH_LpxD, 1 hit
HAMAPiMF_00523, LpxD, 1 hit
InterProiView protein in InterPro
IPR001451, Hexapep
IPR018357, Hexapep_transf_CS
IPR007691, LpxD
IPR011004, Trimer_LpxA-like_sf
IPR020573, UDP_GlcNAc_AcTrfase_non-rep
PANTHERiPTHR43378, PTHR43378, 1 hit
PfamiView protein in Pfam
PF00132, Hexapep, 3 hits
PF04613, LpxD, 1 hit
SUPFAMiSSF51161, SSF51161, 1 hit
TIGRFAMsiTIGR01853, lipid_A_lpxD, 1 hit
PROSITEiView protein in PROSITE
PS00101, HEXAPEP_TRANSFERASES, 4 hits

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 nameiLPXD_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: P21645
<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: May 1, 1991
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 176 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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