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Entry version 23 (11 Dec 2019)
Sequence version 1 (31 Oct 2012)
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Protein

O-antigen chain terminator bifunctional methyltransferase/kinase WbdD

Gene

wbdD

Organism
Escherichia coli
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

Regulates the length of the LPS O-antigen polysaccharide chain. Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar. This terminal modification is essential for export of the O-antigen across the inner membrane. WbdD is also required for correct localization of the WbdA mannosyltransferase.3 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 the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen 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 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 sitei36S-adenosyl-L-methionine2 Publications1
Binding sitei61S-adenosyl-L-methionine; via carbonyl oxygen2 Publications1
Binding sitei128S-adenosyl-L-methionine; via carbonyl oxygen2 Publications1
Binding sitei229ATP; via carbonyl oxygen2 Publications1
Binding sitei237ATP1 Publication1
Binding sitei252ATP2 Publications1
Binding sitei274ATP1 Publication1
Binding sitei358ATP1 Publication1
Binding sitei369ATP2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi241 – 243ATP2 Publications3
Nucleotide bindingi309 – 311ATP2 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Methyltransferase, Transferase
Biological processLipopolysaccharide biosynthesis
LigandATP-binding, Nucleotide-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-20266

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.1.181 2026

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

More...
UniPathwayi
UPA00281

<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:
O-antigen chain terminator bifunctional methyltransferase/kinase WbdDCurated
Including the following 2 domains:
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferaseCurated (EC:2.1.1.2941 Publication)
Polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinaseCurated (EC:2.7.1.1811 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:wbdD1 Publication
<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 coliImported
<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 identifieri562 [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 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, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi16Y → F: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi34N → D: 90% decrease in methyltransferase activity; when associated with E-35 and E-197. 1 Publication1
Mutagenesisi35Q → E: 90% decrease in methyltransferase activity; when associated with D-34 and E-197. 1 Publication1
Mutagenesisi132H → A: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi133H → A: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi197H → E: 90% decrease in methyltransferase activity; when associated with D-34 and E-35. 1 Publication1
Mutagenesisi203R → A: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi230Y → F: Loss of kinase activity. 1 Publication1
Mutagenesisi270R → A: Decrease in kinase activity. 1 Publication1
Mutagenesisi274E → A: Decrease in kinase activity. 1 Publication1
Mutagenesisi350D → A: 10% decrease in kinase activity. 1 Publication1
Mutagenesisi351D → A or E: Loss of kinase activity. 1 Publication1
Mutagenesisi355W → F: Decrease in kinase activity. 1 Publication1
Mutagenesisi355W → H: 50% decrease in kinase 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004306761 – 708O-antigen chain terminator bifunctional methyltransferase/kinase WbdDAdd BLAST708

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer in solution.

Interacts with WbdA.

2 Publications

<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

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
J7I4B7

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 210Methyltransferase2 PublicationsAdd BLAST210
Regioni16 – 17S-adenosyl-L-methionine binding2 Publications2
Regioni82 – 87S-adenosyl-L-methionine binding2 Publications6
Regioni108 – 111S-adenosyl-L-methionine binding2 Publications4
Regioni211 – 459Kinase2 PublicationsAdd BLAST249
Regioni601 – 669Required for membrane-binding1 PublicationAdd BLAST69
Regioni687 – 708Required for localizing WbdA to the membrane1 PublicationAdd BLAST22

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili485 – 594Sequence analysisAdd BLAST110

<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 part contains the methyltransferase and kinase domains that are essential for chain termination and polymer export. The C-terminal region is required for targeting both WbdD and WbdA to the inner membrane.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

Belongs to the WbdD family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K18827

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR025714 Methyltranfer_dom
IPR000719 Prot_kinase_dom
IPR029063 SAM-dependent_MTases

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13847 Methyltransf_31, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53335 SSF53335, 1 hit
SSF56112 SSF56112, 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.

J7I4B7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKDLNTLVS ELPEIYQTIF GHPEWDGDAA RDCNQRLDLI TEQYDNLSRA
60 70 80 90 100
LGRPLNVLDL GCAQGFFSLS LASKGATIVG IDFQQENINV CRALAEENPD
110 120 130 140 150
FAAEFRVGRI EEVIAALEEG EFDLAIGLSV FHHIVHLHGI DEVKRLLSRL
160 170 180 190 200
ADVTQAVILE LAVKEEPFYW GVSQPDDPRE LIEQCAFYRL IGEFDTHLSP
210 220 230 240 250
VPRPMYLVSN HRVLINDFNQ PFQHWQNQPY AGAGLAHKRS RRYFFGEDYV
260 270 280 290 300
CKFFYYDMPH GILTAEESQR NKYELHNEIK FLTQPPAGFD APAVLAHGEN
310 320 330 340 350
AQSGWLVMEK LPGRLLSDML AAGEEIDREK ILGSLLRSLA ALEKQGFWHD
360 370 380 390 400
DVRPWNVMVD ARQHARLIDF GSIVTTPQDC SWPTNLVQSF FVFVNELFAE
410 420 430 440 450
NKSWNGFWRS APVHPFNLPQ PWSNWLYAVW QEPVERWNFV LLLALFEKKA
460 470 480 490 500
KLPSAEQQRG ATEQWIIAQE TVLLELQSRV RNESAGSEAL RGQIHTLEQQ
510 520 530 540 550
MAQLQSAQDA FVEKAQQQVE VSHELTWLGE NMEQLAALLQ TAQAHAQADV
560 570 580 590 600
QPELPPETAE LLQRLEAANR EIHHLSNENQ QLRQEIEKIH RSRSWRMTKG
610 620 630 640 650
YRYLGLQIHL LRQYGFVQRC KHFIKRVLRF VFSFMRKHPQ VKHTAVNGLH
660 670 680 690 700
KLGLYQPAYR LYRRMNPLPH SQYQADAQIL SQTELQVMHP ELLPPEVYEI

YLKLTKNK
Length:708
Mass (Da):81,732
Last modified:October 31, 2012 - 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:i436C35C76096E3F7
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
JX235676 Genomic DNA Translation: AFQ31610.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AFQ31610

<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
JX235676 Genomic DNA Translation: AFQ31610.1

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
4AX8X-ray3.00A2-556[»]
4AZSX-ray2.15A2-556[»]
4AZTX-ray2.34A2-556[»]
4AZVX-ray3.29A2-556[»]
4AZWX-ray2.47A2-458[»]
SMRiJ7I4B7
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

KEGGiag:AFQ31610

Phylogenomic databases

KOiK18827

Enzyme and pathway databases

UniPathwayiUPA00281
BioCyciMetaCyc:MONOMER-20266
BRENDAi2.7.1.181 2026

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR025714 Methyltranfer_dom
IPR000719 Prot_kinase_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF13847 Methyltransf_31, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
SSF56112 SSF56112, 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 nameiWBDD_ECOLX
<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: J7I4B7
<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: October 29, 2014
Last sequence update: October 31, 2012
Last modified: December 11, 2019
This is version 23 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

3D-structure

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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