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Entry version 110 (11 Dec 2019)
Sequence version 1 (08 Nov 2005)
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Protein

3-deoxy-D-manno-octulosonic acid transferase

Gene

waaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.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 <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

Catalytic activity is inhibited by the antibiotic polymixin B and by Re endotoxin.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

  1. KM=52 µM for lipid IV(A) (at pH 8)1 Publication
  2. KM=88 µM for CMP-Kdo (at pH 8)1 Publication
  1. Vmax=18 µmol/min/mg enzyme (at pH 8)1 Publication

pH dependencei

Optimum pH is 7.1 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: KDO(2)-lipid A biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A).1 Publication
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), 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: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei60Proton acceptorBy similarity1
<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>Sitei130Transition state stabilizerBy similarity1
Sitei208Transition state stabilizerBy similarity1

<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

  • 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 functionTransferase
Biological processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:KDOTRANS-MONOMER
ECOL316407:JW3608-MONOMER
MetaCyc:KDOTRANS-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.99.12 2026
2.4.99.13 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0AC75

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

More...
UniPathwayi
UPA00360;UER00483
UPA00360;UER00484
UPA00958

<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:
3-deoxy-D-manno-octulosonic acid transferase (EC:2.4.99.122 Publications, EC:2.4.99.132 Publications)
Short name:
Kdo transferase
Alternative name(s):
Bifunctional Kdo transferase
Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
<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:waaA
Synonyms:kdtA
Ordered Locus Names:b3633, JW3608
<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

  • Cell inner membrane 1 Publication; Single-pass membrane protein 1 Publication; Cytoplasmic side 1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei3 – 23Helical; Signal-anchorSequence analysisAdd 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

Cells lacking this gene display growth defects, absence of Kdo transferase activity, and accumulate massive amounts of lipid IV(A).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_00000802861 – 4253-deoxy-D-manno-octulosonic acid transferaseAdd BLAST425

<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

Degraded by the protease FtsH; therefore FtsH regulates the addition of the sugar moiety to the LPS and thus the maturation of the LPS precursor.1 Publication

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AC75

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

More...
PaxDbi
P0AC75

PRoteomics IDEntifications database

More...
PRIDEi
P0AC75

<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
4263240, 354 interactors
853292, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-48036N

Protein interaction database and analysis system

More...
IntActi
P0AC75, 16 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3633

<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
P0AC75

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

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>Regioni268 – 269CMP-Kdo bindingBy similarity2
Regioni309 – 311CMP-Kdo bindingBy similarity3
Regioni335 – 338CMP-Kdo bindingBy similarity4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal half of KdtA is responsible for determining the number of Kdo residues that are transferred to lipid IVA.1 Publication

<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

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105D8A Bacteria
COG1519 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000257156

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AC75

KEGG Orthology (KO)

More...
KOi
K02527

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AC75

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.11720, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007507 Glycos_transf_N
IPR038107 Glycos_transf_N_sf
IPR039901 Kdotransferase

The PANTHER Classification System

More...
PANTHERi
PTHR42755 PTHR42755, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04413 Glycos_transf_N, 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.

P0AC75-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLELLYTALL YLIQPLIWIR LWVRGRKAPA YRKRWGERYG FYRHPLKPGG
60 70 80 90 100
IMLHSVSVGE TLAAIPLVRA LRHRYPDLPI TVTTMTPTGS ERVQSAFGKD
110 120 130 140 150
VQHVYLPYDL PDALNRFLNK VDPKLVLIME TELWPNLIAA LHKRKIPLVI
160 170 180 190 200
ANARLSARSA AGYAKLGKFV RRLLRRITLI AAQNEEDGAR FVALGAKNNQ
210 220 230 240 250
VTVTGSLKFD ISVTPQLAAK AVTLRRQWAP HRPVWIATST HEGEESVVIA
260 270 280 290 300
AHQALLQQFP NLLLILVPRH PERFPDAINL VRQAGLSYIT RSSGEVPSTS
310 320 330 340 350
TQVVVGDTMG ELMLLYGIAD LAFVGGSLVE RGGHNPLEAA AHAIPVLMGP
360 370 380 390 400
HTFNFKDICA RLEQASGLIT VTDATTLAKE VSSLLTDADY RSFYGRHAVE
410 420
VLYQNQGALQ RLLQLLEPYL PPKTH
Length:425
Mass (Da):47,291
Last modified:November 8, 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:iB063850A1FF392AF
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
M60670 Genomic DNA Translation: AAA24043.1
M86305 Genomic DNA Translation: AAA03745.1
U00039 Genomic DNA Translation: AAB18610.1
U00096 Genomic DNA Translation: AAC76657.1
AP009048 Genomic DNA Translation: BAE77659.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JU0467

NCBI Reference Sequences

More...
RefSeqi
NP_418090.1, NC_000913.3
WP_000891564.1, NZ_STEB01000024.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76657; AAC76657; b3633
BAE77659; BAE77659; BAE77659

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
949048

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3608
eco:b3633

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3073

<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
M60670 Genomic DNA Translation: AAA24043.1
M86305 Genomic DNA Translation: AAA03745.1
U00039 Genomic DNA Translation: AAB18610.1
U00096 Genomic DNA Translation: AAC76657.1
AP009048 Genomic DNA Translation: BAE77659.1
PIRiJU0467
RefSeqiNP_418090.1, NC_000913.3
WP_000891564.1, NZ_STEB01000024.1

3D structure databases

SMRiP0AC75
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4263240, 354 interactors
853292, 1 interactor
DIPiDIP-48036N
IntActiP0AC75, 16 interactors
STRINGi511145.b3633

Proteomic databases

jPOSTiP0AC75
PaxDbiP0AC75
PRIDEiP0AC75

Genome annotation databases

EnsemblBacteriaiAAC76657; AAC76657; b3633
BAE77659; BAE77659; BAE77659
GeneIDi949048
KEGGiecj:JW3608
eco:b3633
PATRICifig|1411691.4.peg.3073

Organism-specific databases

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

More...
EchoBASEi
EB0515

Phylogenomic databases

eggNOGiENOG4105D8A Bacteria
COG1519 LUCA
HOGENOMiHOG000257156
InParanoidiP0AC75
KOiK02527
PhylomeDBiP0AC75

Enzyme and pathway databases

UniPathwayiUPA00360;UER00483
UPA00360;UER00484
UPA00958
BioCyciEcoCyc:KDOTRANS-MONOMER
ECOL316407:JW3608-MONOMER
MetaCyc:KDOTRANS-MONOMER
BRENDAi2.4.99.12 2026
2.4.99.13 2026
SABIO-RKiP0AC75

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0AC75

Family and domain databases

Gene3Di3.40.50.11720, 1 hit
InterProiView protein in InterPro
IPR007507 Glycos_transf_N
IPR038107 Glycos_transf_N_sf
IPR039901 Kdotransferase
PANTHERiPTHR42755 PTHR42755, 1 hit
PfamiView protein in Pfam
PF04413 Glycos_transf_N, 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 nameiKDTA_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: P0AC75
Secondary accession number(s): P23282, Q2M7U7
<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 8, 2005
Last sequence update: November 8, 2005
Last modified: December 11, 2019
This is version 110 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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