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Protein

Rhamnogalacturonan endolyase YesW

Gene

yesW

Organism
Bacillus subtilis (strain 168)
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

Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products (PubMed:16682770, PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin (PubMed:16682770, PubMed:17449691).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

  • Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.2 Publications EC:4.2.2.23

<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

Ca2+4 Publications, Mn2+2 PublicationsNote: Binds 10 calcium ions (PubMed:16682770, PubMed:17449691, PubMed:19193638). The calcium may have a structural role. Requires calcium or manganese for activity (PubMed:16682770, PubMed:17449691).3 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

  1. KM=0.181 mg/ml for rhamnogalacturonan (RG) type I region of plant cell wall pectin1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei152SubstrateCombined sources1 Publication1
    <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 bindingi153Calcium 1Combined sources2 Publications1
    Metal bindingi158Calcium 2Combined sources2 Publications1
    Metal bindingi160Calcium 2Combined sources2 Publications1
    Metal bindingi162Calcium 2Combined sources2 Publications1
    Metal bindingi164Calcium 2; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi166Calcium 2Combined sources2 Publications1
    Binding sitei172SubstrateCombined sources1 Publication1
    Binding sitei187CarbohydrateCombined sources1 Publication1
    Binding sitei207CarbohydrateCombined sources1 Publication1
    Metal bindingi222Calcium 3Combined sources2 Publications1
    Metal bindingi224Calcium 3Combined sources2 Publications1
    Metal bindingi226Calcium 3Combined sources2 Publications1
    Metal bindingi228Calcium 3; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi230Calcium 3Combined sources2 Publications1
    Binding sitei238Carbohydrate; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei255CarbohydrateCombined sources1 Publication1
    Metal bindingi363Calcium 4; via tele nitrogenCombined sources2 Publications1
    Metal bindingi369Calcium 5Combined sources2 Publications1
    Metal bindingi371Calcium 5Combined sources2 Publications1
    Metal bindingi371Calcium 6Combined sources2 Publications1
    Metal bindingi373Calcium 5Combined sources2 Publications1
    Metal bindingi373Calcium 6Combined sources2 Publications1
    Metal bindingi375Calcium 5; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi377Calcium 5Combined sources2 Publications1
    Metal bindingi377Calcium 6Combined sources2 Publications1
    Metal bindingi386Calcium 6Combined sources2 Publications1
    Metal bindingi387Calcium 6; via pros nitrogenCombined sources2 Publications1
    Metal bindingi399Calcium 4; via tele nitrogenCombined sources2 Publications1
    Metal bindingi401Calcium 4Combined sources2 Publications1
    Metal bindingi407Calcium 7Combined sources2 Publications1
    Metal bindingi409Calcium 7; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi412Calcium 7; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi414Calcium 7; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi416Calcium 7Combined sources2 Publications1
    Metal bindingi422Calcium 4Combined sources2 Publications1
    Binding sitei452SubstrateCombined sources2 Publications1
    Metal bindingi457Calcium 8Combined sources2 Publications1
    Metal bindingi459Calcium 8; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi462Calcium 8; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi464Calcium 8; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi466Calcium 8Combined sources2 Publications1
    Metal bindingi496Calcium 9Combined sources2 Publications1
    Metal bindingi498Calcium 9Combined sources2 Publications1
    Metal bindingi500Calcium 9; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi502Calcium 9Combined sources2 Publications1
    Metal bindingi543Calcium 10Combined sources2 Publications1
    Metal bindingi545Calcium 10; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi547Calcium 10; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi549Calcium 10; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi551Calcium 10Combined sources2 Publications1
    Metal bindingi592Calcium 1; via carbonyl oxygenCombined sources2 Publications1
    Metal bindingi594Calcium 1; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei595SubstrateCombined sources2 Publications1
    Metal bindingi596Calcium 1Combined sources2 Publications1

    <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 functionLyase
    Biological processCell wall biogenesis/degradation
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BSUB:BSU07050-MONOMER
    MetaCyc:MONOMER-16263

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.2.23 658

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    O31526

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    PL11 Polysaccharide Lyase Family 11

    <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:
    Rhamnogalacturonan endolyase YesW (EC:4.2.2.232 Publications)
    <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:yesW
    Ordered Locus Names:BSU07050
    <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>OrganismiBacillus subtilis (strain 168)
    <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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <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
    • UP000001570 <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

    <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

    Secreted

    <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>Mutagenesisi363H → A: Strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi399H → A: Strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi401D → N: Strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi422E → Q: Loss of activity. 1 Publication1
    Mutagenesisi452R → A: Strongly reduced catalytic activity and reduced affinity for substrate. 1 Publication1
    Mutagenesisi535K → A: Strongly reduced catalytic activity and reduced affinity for substrate. 1 Publication1
    Mutagenesisi595Y → F: Strongly reduced 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 371 PublicationAdd BLAST37
    <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_000036021238 – 620Rhamnogalacturonan endolyase YesWAdd BLAST583

    Proteomic databases

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

    More...
    PaxDbi
    O31526

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O31526

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated by growth on type I rhamnogalacturonan.1 Publication

    <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

    Monomer.3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    224308.Bsubs1_010100003963

    <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

    1620
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O31526

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

    More...
    SMRi
    O31526

    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
    O31526

    <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>Regioni532 – 534Substrate bindingCombined sources1 Publication3

    <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

    Rhamnose is bound near the active site, but there are also additional rhamnose-binding sites far away from the active site, which possibly function as a carbohydrate-binding region.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 polysaccharide lyase 11 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CX8 Bacteria
    ENOG410XPAI LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000251614

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O31526

    KEGG Orthology (KO)

    More...
    KOi
    K18197

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YTQFQVY

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O31526

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd10318 RGL11, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.60.40.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013783 Ig-like_fold
    IPR034641 RGL11

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43118 PTHR43118, 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.

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

    O31526-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRRSCLMIRR RKRMFTAVTL LVLLVMGTSV CPVKAEGAAR QMEALNRGLV
    60 70 80 90 100
    AVKTDGGIFV SWRFLGTENA SVLFNVYRDG QKLNAAPVKT TNYVDKNGSA
    110 120 130 140 150
    GSTYTVRAVV NGTEQPASEK ASVWAQPYHS VPLDKPAGGT TPKGESYTYS
    160 170 180 190 200
    ANDASVGDVD GDGQYELILK WDPSNSKDNS QDGYTGDVLI DAYKLDGTKL
    210 220 230 240 250
    WRINLGKNIR AGAHYTQFMV YDLDGDGKAE VAMKTADGTK DGTGKVIGNA
    260 270 280 290 300
    NADYRNEQGR VLSGPEYLTV FQGSTGKELV TANFEPARGN VSDWGDSYGN
    310 320 330 340 350
    RVDRFLAGIA YLDGQRPSLI MTRGYYAKTM LVAYNFRDGK LSKLWTLDSS
    360 370 380 390 400
    KSGNEAFAGQ GNHNLSIADV DGDGKDEIIF GSMAVDHDGK GMYSTGLGHG
    410 420 430 440 450
    DALHTGDLDP GRPGLEVFQV HEDKNAKYGL SFRDAATGKI LWGVYAGKDV
    460 470 480 490 500
    GRGMAADIDP RYPGQEVWAN GSLYSAKGVK IGSGVPSSTN FGIWWDGDLL
    510 520 530 540 550
    REQLDSNRID KWDYQNGVSK NMLTASGAAA NNGTKATPTL QADLLGDWRE
    560 570 580 590 600
    EVVWRTEDSS ALRIYTTTIP TEHRLYTLMH DPVYRLGIAW QNIAYNQPPH
    610 620
    TSFFLGDGMA EQPKPNMYTP
    Length:620
    Mass (Da):67,587
    Last modified:January 1, 1998 - 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:iD4573AF7B3E9358D
    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
    AL009126 Genomic DNA Translation: CAB12524.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F69797

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_388586.1, NC_000964.3
    WP_010886436.1, NZ_JNCM01000032.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB12524; CAB12524; BSU07050

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    938769

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bsu:BSU07050

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224308.43.peg.743

    <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
    AL009126 Genomic DNA Translation: CAB12524.1
    PIRiF69797
    RefSeqiNP_388586.1, NC_000964.3
    WP_010886436.1, NZ_JNCM01000032.1

    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
    2Z8RX-ray1.40A/B38-620[»]
    2Z8SX-ray2.50A/B38-620[»]
    2ZUXX-ray1.32A/B38-620[»]
    ProteinModelPortaliO31526
    SMRiO31526
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100003963

    Protein family/group databases

    CAZyiPL11 Polysaccharide Lyase Family 11

    Proteomic databases

    PaxDbiO31526
    PRIDEiO31526

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB12524; CAB12524; BSU07050
    GeneIDi938769
    KEGGibsu:BSU07050
    PATRICifig|224308.43.peg.743

    Phylogenomic databases

    eggNOGiENOG4105CX8 Bacteria
    ENOG410XPAI LUCA
    HOGENOMiHOG000251614
    InParanoidiO31526
    KOiK18197
    OMAiYTQFQVY
    PhylomeDBiO31526

    Enzyme and pathway databases

    BioCyciBSUB:BSU07050-MONOMER
    MetaCyc:MONOMER-16263
    BRENDAi4.2.2.23 658
    SABIO-RKiO31526

    Miscellaneous databases

    EvolutionaryTraceiO31526

    Family and domain databases

    CDDicd10318 RGL11, 1 hit
    Gene3Di2.60.40.10, 1 hit
    InterProiView protein in InterPro
    IPR013783 Ig-like_fold
    IPR034641 RGL11
    PANTHERiPTHR43118 PTHR43118, 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 nameiYESW_BACSU
    <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: O31526
    <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: January 20, 2009
    Last sequence update: January 1, 1998
    Last modified: December 5, 2018
    This is version 97 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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