Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 73 (07 Apr 2021)
Sequence version 1 (01 Jun 2001)
Previous versions | rss
Add a publicationFeedback
Protein

Chaplin-H

Gene

chpH

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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

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). Chaplins are also involved in cell attachment to a hydrophobic surface (PubMed:19682261). Forms amyloid fibrils in vitro probably composed of stacked beta-sheets (PubMed:21526199). A small chaplin extract (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles into 2 different amyloids; small fibrils at the air-water interface form an amiphipathic membrane that resembles spore-surface structures involved in aerial hyphae formation, and hydrophilic fibrils in solution that resemble the fibers that attach cells to a hydrophobic surface. At the air-water interface the hydrophilic surface is in contact with water (probably equivalent to the peptidoglycan layer), while the hydrophobic face is exposed to the air, making the surface of the aerial hyphae hydrophobic (PubMed:24012833). A minimal chaplin strain capable of forming aerial mycelium/hyphae on minimal medium contains ChpC, ChpE and ChpH. The strain also has restored rodlet formation on the hyphae surface (PubMed:18586935). A small chaplin extract applied to a chaplin-deficient strain restores aerial hyphae formation (PubMed:12832396, PubMed:12832397). The small chaplin extract forms an amyloid-like structure similar to that seen on the surface of cells without rodlets (rdlA-rdlB deletions), and is highly surface active, reducing surface tension from 72 to 26 mJ/m2, which probably allows escape of hyphae from an aqueous environment into air (PubMed:12832396).8 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 - Molecular functioni

  • identical protein binding Source: IntAct

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

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-H1 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:chpH1 Publication
Ordered Locus Names:SCO1675
<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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces 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, Fimbrium, 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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

The small chaplin mixture (a cell wall extract of an rdlA-rdlB knockout) forms a stable coat on a number of surfaces (including Teflon and cotton) and emulsifies oil-water mixtures, which could be useful in medical and technical applications.1 Publication

<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 chpH disruption and double chpC-chpH knockout have no visible or sporulation 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 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 attachment (PubMed:19682261).5 Publications

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>Mutagenesisi30 – 51Missing : Very decreased formation of aerial hyphae, no spore chains formed, no effect on rodlet formation. 1 PublicationAdd BLAST22
Mutagenesisi56C → V in minimal chaplin strain, forms very sparse aerial hyphae, no rodlets form; when associated with G-74, loss of disulfide bond. 1 Publication1
Mutagenesisi62 – 66VIGLL → AAAAA: Severely reduced ability to form amyloid fibers in vitro, very decreased formation of aerial hyphae, very few rodlets, no spore chains formed. 1 Publication5
Mutagenesisi62V → A: Significantly reduced ability to form amyloid fibers in vitro, decreased formation of aerial hyphae and rodlets, no change in spore chain formation. 1 Publication1
Mutagenesisi74C → G in minimal chaplin strain, forms very sparse aerial hyphae, no rodlets form; when associated with V-56, loss of disulfide bond. 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 – 252 PublicationsAdd BLAST25
<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_500432394026 – 77Chaplin-HSequence analysisAdd BLAST52

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi56 ↔ 742 Publications

Keywords - PTMi

Disulfide bond

<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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Present in aerial hyphae of sporulating cultures (at protein level) (PubMed:12832396, PubMed:17462011). Strongest expression in spores, with weaker expression in aerial hyphae (PubMed:12832397).3 Publications

<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

Highly expressed in 24 hour cultures while still submerged, during aerial hyphae formation on minimal medium, decreases once aerial growth ceases. Strongly expressed in aerial hyphae (at protein level) (PubMed:12832396). During aerial hyphae formation and sporulation on rich medium, under control of ECF sigma factor BldN; more strongly expressed when sporulation is blocked by deletion of whiB, whiD or whiH (PubMed:12832397). Expression depends on bldB but not bldA, bldD or bldH (at protein level) (PubMed:17462011).3 Publications

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide linked. About 10% of ChpH isolated from cell wall forms disulfide-bonded homodimers.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q9AD92
With#Exp.IntAct
itself2EBI-15929047,EBI-15929047

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-60401N

STRING: functional protein association networks

More...
STRINGi
100226.SCO1675

<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>Domaini36 – 76ChaplinPROSITE-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>Regioni38 – 54Forms amyloid fibrils in vitro1 PublicationAdd BLAST17
Regioni57 – 72Forms amyloid fibrils in vitro1 PublicationAdd BLAST16

<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

Has 2 domains capable of forming beta amyloid structures, both of which are required for aerial hyphae formation while the N-terminal region is not required for rodlet formation.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 chaplin family. Short chaplin subfamily.1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG50348JU, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_145456_3_1_11

Identification of Orthologs from Complete Genome Data

More...
OMAi
VHSPGVV

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9AD92

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03777, ChpA-C, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51884, CHAPLIN, 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.

Q9AD92-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLKKVVAAAA ATGGLVLAGA GMAVADSGAQ GAAVHSPGVL SGNVVQVPVH
60 70
VPVNVCGNTI SVIGLLNPAF GNVCINK
Length:77
Mass (Da):7,345
Last modified:June 1, 2001 - 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:i34FAD03DBE797735
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 5122 Da. Determined by MALDI. 1 Publication
Molecular mass is 5116.61 Da. Determined by MALDI. 1 Publication

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
AL939109 Genomic DNA Translation: CAC36378.1

NCBI Reference Sequences

More...
RefSeqi
NP_625950.1, NC_003888.3
WP_003977150.1, NZ_VNID01000018.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1097106

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sco:SCO1675

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|100226.15.peg.1692

<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
AL939109 Genomic DNA Translation: CAC36378.1
RefSeqiNP_625950.1, NC_003888.3
WP_003977150.1, NZ_VNID01000018.1

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

DIPiDIP-60401N
STRINGi100226.SCO1675

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1097106

Genome annotation databases

GeneIDi1097106
KEGGisco:SCO1675
PATRICifig|100226.15.peg.1692

Phylogenomic databases

eggNOGiENOG50348JU, Bacteria
HOGENOMiCLU_145456_3_1_11
OMAiVHSPGVV
PhylomeDBiQ9AD92

Family and domain databases

InterProiView protein in InterPro
IPR005528, ChpA-H
PfamiView protein in Pfam
PF03777, ChpA-C, 1 hit
PROSITEiView protein in PROSITE
PS51884, CHAPLIN, 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 nameiCHPH_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: Q9AD92
<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: June 1, 2001
Last modified: April 7, 2021
This is version 73 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again