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Entry version 66 (12 Aug 2020)
Sequence version 1 (24 Mar 2009)
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Protein

Undecaprenyl-diphosphooligosaccharide--protein glycotransferase

Gene

pglB

Organism
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
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

Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (GalNAc2GlcGalNAc3Bac(NAc)2 in eubacteria, where Bac(NAc)2 is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.2 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+2 Publications

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

Glycosylates at a rate of 1.55 peptides per second per OST.1 Publication
  1. KM=2.6 µM for an Asp-Gln-Asn-Ala-Thr pentapeptide1 Publication

    pH dependencei

    Optimum pH is 6.8.1 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: protein glycosylation

    This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
    View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi56Manganese1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei56Target acceptor peptide1 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>Sitei147Important for catalytic activity1 Publication1
    Metal bindingi154Manganese1 Publication1
    Binding sitei293Lipid-linked oligosaccharide1 Publication1
    Metal bindingi319Manganese1 Publication1
    Binding sitei319Target acceptor peptide1 Publication1
    Binding sitei331Target acceptor peptide; important for extended sequon recognition1 Publication1
    Binding sitei375Lipid-linked oligosaccharide1 Publication1
    Binding sitei468Lipid-linked oligosaccharide1 Publication1
    Binding sitei572Target acceptor peptide1 Publication1

    <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 functionGlycosyltransferase, Transferase
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    CLAR306263:G1GB2-1254-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.4.99.19, 13108

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

    More...
    UniPathwayi
    UPA00378

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GT66, Glycosyltransferase Family 66

    Transport Classification Database

    More...
    TCDBi
    9.B.142.3.11, the integral membrane glycosyltransferase family 39 (gt39) family

    <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:
    Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC:2.4.99.19)
    Alternative name(s):
    Protein glycosylation B
    <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:pglB
    Ordered Locus Names:Cla_1253
    <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>OrganismiCampylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
    <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 identifieri306263 [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 lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    <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
    • UP000007727 <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

    <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 subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 12Cytoplasmic1 PublicationAdd BLAST12
    <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>Transmembranei13 – 37Helical1 PublicationAdd BLAST25
    Topological domaini38 – 98Periplasmic1 PublicationAdd BLAST61
    Transmembranei99 – 124Helical1 PublicationAdd BLAST26
    Topological domaini125 – 127Cytoplasmic1 Publication3
    Transmembranei128 – 146Helical1 PublicationAdd BLAST19
    Topological domaini147 – 154Periplasmic1 Publication8
    Transmembranei155 – 176Helical1 PublicationAdd BLAST22
    Topological domaini177 – 178Cytoplasmic1 Publication2
    Transmembranei179 – 194Helical1 PublicationAdd BLAST16
    Topological domaini195 – 199Periplasmic1 Publication5
    Transmembranei200 – 217Helical1 PublicationAdd BLAST18
    Topological domaini218 – 222Cytoplasmic1 Publication5
    Transmembranei223 – 235Helical1 PublicationAdd BLAST13
    Topological domaini236 – 239Periplasmic1 Publication4
    Transmembranei240 – 256Helical1 PublicationAdd BLAST17
    Topological domaini257 – 262Cytoplasmic1 Publication6
    Transmembranei263 – 280Helical1 PublicationAdd BLAST18
    Topological domaini281 – 327Periplasmic1 PublicationAdd BLAST47
    Transmembranei328 – 350Helical1 PublicationAdd BLAST23
    Topological domaini351 – 355Cytoplasmic1 Publication5
    Transmembranei356 – 372Helical1 PublicationAdd BLAST17
    Topological domaini373 – 376Periplasmic1 Publication4
    Transmembranei377 – 399Helical1 PublicationAdd BLAST23
    Topological domaini400 – 407Cytoplasmic1 Publication8
    Transmembranei408 – 432Helical1 PublicationAdd BLAST25
    Topological domaini433 – 712Periplasmic1 PublicationAdd BLAST280

    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%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>Mutagenesisi56D → A: Strongly reduced catalytic activity. Abolished catalytic activity; when associated with A-319. 1 Publication1
    Mutagenesisi154D → A: Reduced catalytic activity. 1 Publication1
    Mutagenesisi196Y → A or F: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi319E → A: Strongly reduced catalytic activity. Abolished catalytic activity; when associated with A-56. 1 Publication1
    Mutagenesisi468Y → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi468Y → F: Reduces catalytic 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_00004225891 – 712Undecaprenyl-diphosphooligosaccharide--protein glycotransferaseAdd BLAST712

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi535N-linked (DATDGlc) asparagine1 Publication1
    Glycosylationi556N-linked (DATDGlc) asparagine1 Publication1

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    B9KDD4

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    B9KDD4

    <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

    Database of interacting proteins

    More...
    DIPi
    DIP-59188N

    STRING: functional protein association networks

    More...
    STRINGi
    306263.Cla_1253

    <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

    1712
    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
    B9KDD4

    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>Regioni196 – 198Lipid-linked oligosaccharide binding1 Publication3
    Regioni463 – 465Target acceptor peptide binding1 Publication3

    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>Motifi54 – 56DXD motif 1Sequence analysis3
    Motifi154 – 156DXD motif 21 Publication3
    Motifi316 – 319TIXE motifBy similarity4
    Motifi463 – 467WWDYG motifBy similarity5
    Motifi569 – 576MI motifBy similarity8

    <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

    Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.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 STT3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG1287, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_024679_0_0_7

    KEGG Orthology (KO)

    More...
    KOi
    K17251

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GYPIRYY

    Database of Orthologous Groups

    More...
    OrthoDBi
    702825at2

    Family and domain databases

    Database of protein disorder

    More...
    DisProti
    DP01199

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003674, Oligo_trans_STT3
    IPR041563, STT3_PglB_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02516, STT3, 1 hit
    PF18527, STT3_PglB_C, 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.

    B9KDD4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKLQQNFTDN NSIKYTCILI LIAFAFSVLC RLYWVAWASE FYEFFFNDQL
    60 70 80 90 100
    MITTNDGYAF AEGARDMIAG FHQPNDLSYF GSSLSTLTYW LYSILPFSFE
    110 120 130 140 150
    SIILYMSAFF ASLIVVPIIL IAREYKLTTY GFIAALLGSI ANSYYNRTMS
    160 170 180 190 200
    GYYDTDMLVL VLPMLILLTF IRLTINKDIF TLLLSPVFIM IYLWWYPSSY
    210 220 230 240 250
    SLNFAMIGLF GLYTLVFHRK EKIFYLTIAL MIIALSMLAW QYKLALIVLL
    260 270 280 290 300
    FAIFAFKEEK INFYMIWALI FISILILHLS GGLDPVLYQL KFYVFKASDV
    310 320 330 340 350
    QNLKDAAFMY FNVNETIMEV NTIDPEVFMQ RISSSVLVFI LSFIGFILLC
    360 370 380 390 400
    KDHKSMLLAL PMLALGFMAL RAGLRFTIYA VPVMALGFGY FLYAFFNFLE
    410 420 430 440 450
    KKQIKLSLRN KNILLILIAF FSISPALMHI YYYKSSTVFT SYEASILNDL
    460 470 480 490 500
    KNKAQREDYV VAWWDYGYPI RYYSDVKTLI DGGKHLGKDN FFSSFVLSKE
    510 520 530 540 550
    QIPAANMARL SVEYTEKSFK ENYPDVLKAM VKDYNKTSAK DFLESLNDKD
    560 570 580 590 600
    FKFDTNKTRD VYIYMPYRML RIMPVVAQFA NTNPDNGEQE KSLFFSQANA
    610 620 630 640 650
    IAQDKTTGSV MLDNGVEIIN DFRALKVEGA SIPLKAFVDI ESITNGKFYY
    660 670 680 690 700
    NEIDSKAQIY LLFLREYKSF VILDESLYNS SYIQMFLLNQ YDQDLFEQIT
    710
    NDTRAKIYRL KR
    Length:712
    Mass (Da):82,729
    Last modified:March 24, 2009 - 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:iA04C959507F3C581
    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
    CP000932 Genomic DNA Translation: ACM64573.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012661956.1, NC_012039.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ACM64573; ACM64573; Cla_1253

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    7410986

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cla:CLA_1253

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|306263.5.peg.1240

    <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
    CP000932 Genomic DNA Translation: ACM64573.1
    RefSeqiWP_012661956.1, NC_012039.1

    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
    3RCEX-ray3.40A1-712[»]
    5OGLX-ray2.70A1-712[»]
    6GXCX-ray3.40A1-712[»]
    SMRiB9KDD4
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    DIPiDIP-59188N
    STRINGi306263.Cla_1253

    Protein family/group databases

    CAZyiGT66, Glycosyltransferase Family 66
    TCDBi9.B.142.3.11, the integral membrane glycosyltransferase family 39 (gt39) family

    PTM databases

    iPTMnetiB9KDD4

    Proteomic databases

    PRIDEiB9KDD4

    Genome annotation databases

    EnsemblBacteriaiACM64573; ACM64573; Cla_1253
    GeneIDi7410986
    KEGGicla:CLA_1253
    PATRICifig|306263.5.peg.1240

    Phylogenomic databases

    eggNOGiCOG1287, Bacteria
    HOGENOMiCLU_024679_0_0_7
    KOiK17251
    OMAiGYPIRYY
    OrthoDBi702825at2

    Enzyme and pathway databases

    UniPathwayiUPA00378
    BioCyciCLAR306263:G1GB2-1254-MONOMER
    BRENDAi2.4.99.19, 13108

    Family and domain databases

    DisProtiDP01199
    InterProiView protein in InterPro
    IPR003674, Oligo_trans_STT3
    IPR041563, STT3_PglB_C
    PfamiView protein in Pfam
    PF02516, STT3, 1 hit
    PF18527, STT3_PglB_C, 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 nameiPGLB_CAMLR
    <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: B9KDD4
    <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 29, 2013
    Last sequence update: March 24, 2009
    Last modified: August 12, 2020
    This is version 66 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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