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Entry version 67 (05 Dec 2018)
Sequence version 1 (15 Feb 2005)
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Protein

Undecaprenyl-diphosphooligosaccharide--protein glycotransferase

Gene

pglB

Organism
Campylobacter jejuni (strain RM1221)
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

Oligosaccharyltransferase that catalyzes the transfer of a preassembled heptasaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains, affording a beta-linked glycan to the asparagine side chain of target proteins.1 Publication
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.By similarity

<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

  • Tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine.1 Publication EC:2.4.99.19

<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+By similarity, Mn2+By similarity

<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: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarity
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 ‘Function’ 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 bindingi54ManganeseBy similarity1
<p>This subsection of the ‘Function’ 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 sitei54Target acceptor peptideBy 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>Sitei145Important for catalytic activityBy similarity1
Metal bindingi152ManganeseBy similarity1
Binding sitei291Lipid-linked oligosaccharideBy similarity1
Metal bindingi316ManganeseBy similarity1
Binding sitei316Target acceptor peptideBy similarity1
Binding sitei328Target acceptor peptide; important for extended sequon recognitionBy similarity1
Binding sitei372Lipid-linked oligosaccharideBy similarity1
Binding sitei462Lipid-linked oligosaccharideBy similarity1
Binding sitei571Target acceptor peptideBy 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

  • metal ion binding Source: UniProtKB-KW
  • oligosaccharyl transferase activity Source: InterPro
  • transferase activity, transferring glycosyl groups Source: TIGR

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, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
CJEJ195099:G1G43-1269-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.99.18 1087
2.4.99.19 1087

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

<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:
Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC:2.4.99.191 Publication)
Alternative name(s):
Protein glycosylation B
<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:pglB
Ordered Locus Names:CJE1268
<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>OrganismiCampylobacter jejuni (strain RM1221)
<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 identifieri195099 [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 lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

<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_location_section">'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 – 11CytoplasmicCuratedAdd BLAST11
<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>Transmembranei12 – 35HelicalBy similarityAdd BLAST24
Topological domaini36 – 96PeriplasmicCuratedAdd BLAST61
Transmembranei97 – 122HelicalBy similarityAdd BLAST26
Topological domaini123 – 125CytoplasmicCurated3
Transmembranei126 – 144HelicalBy similarityAdd BLAST19
Topological domaini145 – 152PeriplasmicCurated8
Transmembranei153 – 174HelicalBy similarityAdd BLAST22
Topological domaini175 – 176CytoplasmicCurated2
Transmembranei177 – 192HelicalBy similarityAdd BLAST16
Topological domaini193 – 197PeriplasmicCurated5
Transmembranei198 – 215HelicalBy similarityAdd BLAST18
Topological domaini216 – 220CytoplasmicCurated5
Transmembranei221 – 233HelicalBy similarityAdd BLAST13
Topological domaini234 – 237PeriplasmicCurated4
Transmembranei238 – 254HelicalBy similarityAdd BLAST17
Topological domaini255 – 260CytoplasmicCurated6
Transmembranei261 – 278HelicalBy similarityAdd BLAST18
Topological domaini279 – 324PeriplasmicCuratedAdd BLAST46
Transmembranei325 – 347HelicalBy similarityAdd BLAST23
Topological domaini348 – 352CytoplasmicCurated5
Transmembranei353 – 369HelicalBy similarityAdd BLAST17
Topological domaini370 – 373PeriplasmicCurated4
Transmembranei374 – 396HelicalBy similarityAdd BLAST23
Topological domaini397 – 406CytoplasmicCurated10
Transmembranei407 – 427HelicalBy similarityAdd BLAST21
Topological domaini428 – 713PeriplasmicCuratedAdd BLAST286

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>Mutagenesisi52S → E or D: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi53N → A: Reduced catalytic activity. 1 Publication1
Mutagenesisi54D → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi568M → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi569S → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi570L → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi571I → A: Strong reduction in 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004225881 – 713Undecaprenyl-diphosphooligosaccharide--protein glycotransferaseAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi534N-linked (DATDGlc) asparagineBy similarity1

Keywords - PTMi

Glycoprotein

<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

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
3AAGX-ray2.80A/B428-713[»]

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

More...
SMRi
Q5HTX9

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q5HTX9

<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>Regioni194 – 196Lipid-linked oligosaccharide bindingBy similarity3
Regioni457 – 459Target acceptor peptide bindingBy similarity3

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>Motifi52 – 54DXD motif 11 Publication3
Motifi152 – 154DXD motif 21 Publication3
Motifi313 – 316TIXE motif1 Publication4
Motifi457 – 461WWDYG motif1 Publication5
Motifi568 – 575MI 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.By similarity

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000103852

KEGG Orthology (KO)

More...
KOi
K17251

Identification of Orthologs from Complete Genome Data

More...
OMAi
GYPIRYY

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003674 Oligo_trans_STT3

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02516 STT3, 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>.<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.

Q5HTX9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLKKEYLKNP YLVLFAMIIL AYVFSVLCRF YWIWWASEFN EYFFNNQLMI
60 70 80 90 100
ISNDGYAFAE GARDMIAGFH QPNDLSYYGS SLSTLTYWLY KITPFSFESI
110 120 130 140 150
ILYMSTFLSS LVVIPIILLA NEYKRPLMGF VAALLASVAN SYYNRTMSGY
160 170 180 190 200
YDTDMLVIVL PMFILFFMVR MILKKDFFSL IALPLFIGIY LWWYPSSYTL
210 220 230 240 250
NVALIGLFLI YTLIFHRKEK IFYIAVILSS LTLSNIAWFY QSAIIVILFA
260 270 280 290 300
LFALEQKRLN FMIIGILGSA TLIFLILSGG VDPILYQLKF YIFRNDESAN
310 320 330 340 350
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH
360 370 380 390 400
KSMIMALPIL VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY
410 420 430 440 450
SQLTSNVCIV FATILTLAPV FIHIYNYKAP TVFSQNEASL LNQLKNIANR
460 470 480 490 500
EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL GKDNFFPSFA LSKDEQAAAN
510 520 530 540 550
MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL FLASLSKPDF
560 570 580 590 600
KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL
610 620 630 640 650
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI
660 670 680 690 700
DDKAQFYIFY LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV
710
INSRDAKVFK LKI
Length:713
Mass (Da):82,206
Last modified:February 15, 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:iB5D4836BF36D8FF8
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
CP000025 Genomic DNA Translation: AAW35590.1

NCBI Reference Sequences

More...
RefSeqi
WP_011049884.1, NC_003912.7

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAW35590; AAW35590; CJE1268

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cjr:CJE1268

<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
CP000025 Genomic DNA Translation: AAW35590.1
RefSeqiWP_011049884.1, NC_003912.7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AAGX-ray2.80A/B428-713[»]
SMRiQ5HTX9
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT66 Glycosyltransferase Family 66

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW35590; AAW35590; CJE1268
KEGGicjr:CJE1268

Phylogenomic databases

HOGENOMiHOG000103852
KOiK17251
OMAiGYPIRYY

Enzyme and pathway databases

UniPathwayi
UPA00378

BioCyciCJEJ195099:G1G43-1269-MONOMER
BRENDAi2.4.99.18 1087
2.4.99.19 1087

Miscellaneous databases

EvolutionaryTraceiQ5HTX9

Family and domain databases

InterProiView protein in InterPro
IPR003674 Oligo_trans_STT3
PfamiView protein in Pfam
PF02516 STT3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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_CAMJR
<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: Q5HTX9
<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: May 29, 2013
Last sequence update: February 15, 2005
Last modified: December 5, 2018
This is version 67 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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