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UniProtKB - Q9X7U2 (CHPB_STRCO)

Entry version 89 (23 Feb 2022)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
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Protein

Chaplin-B

Gene

chpB

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score:

Annotation score:3 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

One of 8 partially redundant surface-active proteins required for efficient formation of aerial mycelium; the short chaplins assemble into a hydrophobic, amyloidal fibrillar surface layer that envelopes and protects aerial hyphae and spores, presumably anchored to the long chaplins (PubMed:12832396, PubMed:12832397, PubMed:15228525, PubMed:17462011).

Chaplins have an overlapping function with the surface-active SapB peptide; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation (PubMed:17462011).

The long chaplins (ChpA, ChpB, ChpC) are not absolutely necessary for short chaplin localization or rodlet formation, but probably play a role in initiating aerial hyphae development (PubMed:22296345).

Chaplins are also involved in cell attachment to a hydrophobic surface (PubMed:19682261).

6 Publications

<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 - Biological processi

Complete GO annotation on QuickGO ...

<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

Biological processCell adhesion

<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:
Chaplin-B1 Publication
<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:chpB1 Publication
Ordered Locus Names:SCO7257
<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>OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
<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 identifieri100226 [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 lineageiBacteria › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces › Streptomyces albidoflavus group ›
<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
  • UP000001973 <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

Keywords - Cellular componenti

Amyloid, Cell wall, 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

A single chpB disruption has no phenotype; a quadruple chpA-chpC-chpD-chpH knockout has delayed aerial hyphae formation and sporulation. A quintuple chpA-chpB-chpC-chpD-chpH knockout has a longer delay in aerial hyphae formation and an almost complete lack of sporulation. The quintuple knockout still expresses ChpE, ChpF and ChpG (PubMed:12832397). Quintuple knockout chpA-chpB-chpC-chpD-chpH has strongly delayed aerial hyphae formation, makes many fewer aerial hyphae but no effect on viability of the spores produced. Further deletion of chpE leads to more severe effects, and on rich media few aerial hyphae are produced after prolonged growth. Those few hyphae do differentiate into spores and have a rodlet layer (PubMed:12832396). Deletion of all 8 chaplin genes on minimal medium leads to severely disrupted aerial hyphae that collapse on the colony surface and are not hydrophobic. A few spore chains can still be made, but they have neither rodlets or amyloid-like fibers. rdlA and rdlB mRNA are down-regulated (PubMed:15228525, PubMed:17462011). Deletion of all 8 chaplin genes on rich medium leads to a reduced abundance of aerial hyphae without rodlets and occasional spore chains on surface hyphae. A complete chaplin-negative plus ram-negative strain (deletion of ramR or the ramC-ramS-ramA-ramB operon) leads to the complete loss of robust aerial hyphae (PubMed:17462011). Deletion of the 3 long chaplins (ChpA, ChpB, ChpC) results in a 24 hour delay in aerial hyphae formation, while rodlets are about 1.5-fold longer than wild-type (PubMed:22296345). Deletion of all 8 chaplin genes significantly reduces cellular attachment to a hydrophobic substrate; thin fibrils instead of fimbrae are detected. The long chaplins (ChpA, ChpB and ChpC, as seen by near wild-type attachment of the hextuple chpA-chpB-chpC-chpD-chpE-chpH knockout) are not essential but may contribute to cellular attachment (PubMed:19682261).6 Publications

<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 – 26Sequence analysisAdd BLAST26
<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_500433627527 – 237Chaplin-BSequence analysisAdd BLAST211
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000445189206 – 237Removed by sortasePROSITE-ProRule annotationAdd BLAST32

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei205Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

Keywords - PTMi

Peptidoglycan-anchor

<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

Transcribed during aerial hyphae formation on minimal medium, about 10- to 25-fold lower expression than the short chaplins. Weak expression in aerial hyphae (at protein level) (Probable). Very low expression on rich medium, unaffected by ECF sigma factor BldN (PubMed:12832397).1 Publication1 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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		100226.SCO7257

<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

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini42 – 82Chaplin 1PROSITE-ProRule annotationAdd BLAST41
Domaini120 – 160Chaplin 2PROSITE-ProRule annotationAdd BLAST41

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>Regioni81 – 127DisorderedSequence analysisAdd BLAST47
Regioni148 – 216DisorderedSequence analysisAdd BLAST69

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>Motifi202 – 206LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi93 – 109Polar residuesSequence analysisAdd BLAST17
Compositional biasi148 – 162Polar residuesSequence analysisAdd BLAST15
Compositional biasi163 – 181Basic and acidic residuesSequence analysisAdd BLAST19

<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 chaplin family. Long chaplin subfamily.1 Publication

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG5034C0V, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_070271_0_0_11

Identification of Orthologs from Complete Genome Data

More...OMAi		RRTEDRI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005528, ChpA-H
IPR019931, LPXTG_anchor

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03777, ChpA-C, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51884, CHAPLIN, 2 hits
PS50847, GRAM_POS_ANCHORING, 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.

<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 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.

Q9X7U2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRVTRNGVL AVAASGALAV TMPAYAAFAS DGAGAEGSAA GSPGLISGNT 
        60         70         80         90        100
VQLPVDVPVD VCGNTVNVVG LLNPAAGNGC ADSGEPGASY QAAGASGGTS 
       110        120        130        140        150
GSATEATSGG AAAEGSGKDS PGVLSGNGVQ LPVHLPVNVS GNSVNVVGIG 
       160        170        180        190        200
NPAVGNESTN DSGDHPEPVR PPAEPEPSAP EEERAGPGPS AHAAPPREEV 
       210        220        230 
SLAHTGTDRT LPTLAGGAAL VLGGTVLYRR FRPGSGD
Length:237
Mass (Da):22,741
Last modified:November 1, 1999 - 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:i73E3C5F2A0C745AF
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
AL939131 Genomic DNA Translation: CAB42960.1

Protein sequence database of the Protein Information Resource

More...PIRi		T35351

NCBI Reference Sequences

More...RefSeqi		NP_631313.1, NC_003888.3
WP_011031547.1, NC_003888.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1102695

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sco:SCO7257

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|100226.15.peg.7359

<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
AL939131 Genomic DNA Translation: CAB42960.1
PIRiT35351
RefSeqiNP_631313.1, NC_003888.3
WP_011031547.1, NC_003888.3

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Protein-protein interaction databases

STRINGi100226.SCO7257

Genome annotation databases

GeneIDi1102695
KEGGisco:SCO7257
PATRICifig|100226.15.peg.7359

Phylogenomic databases

eggNOGiENOG5034C0V, Bacteria
HOGENOMiCLU_070271_0_0_11
OMAiRRTEDRI

Family and domain databases

InterProiView protein in InterPro
IPR005528, ChpA-H
IPR019931, LPXTG_anchor
PfamiView protein in Pfam
PF03777, ChpA-C, 2 hits
PROSITEiView protein in PROSITE
PS51884, CHAPLIN, 2 hits
PS50847, GRAM_POS_ANCHORING, 1 hit

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 nameiCHPB_STRCO
<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: Q9X7U2
<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: October 10, 2018
Last sequence update: November 1, 1999
Last modified: February 23, 2022
This is version 89 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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