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 35 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

ESAT-6-like protein EsxB

Gene

esxB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

A secreted protein. Acts as a strong host (human) T-cell antigen (PubMed:11940590). Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm (PubMed:17604718). Might serve as a chaperone to prevent uncontrolled membrane lysis by its partner EsxA; native protein binds poorly to artificial liposomes in the absence or presence of EsxA (PubMed:17557817, PubMed:26260636). EsxA and EsxA-EsxB are cytotoxic to pneumocytes (PubMed:19906174). EsxB (and EsxA-EsxB but not EsxA alone) activates human neutrophils; EsxB transiently induces host (human) intracellular Ca2+ mobility in a dose-dependent manner, monocytes and lymphocytes do not respond (PubMed:25332123). Neutrophils respond to EsxB by chemotaxis and primed neutrophils treated with EsxB produce reactive oxygen species (ROS); Ca2+ release and the ROS burst via are induced by an unidentified G-protein coupled receptor (PubMed:25332123). May help regulate assembly and function of the type VII secretion system (T7SS) (PubMed:25865481).1 Publication6 Publications

Miscellaneous

Genes esxA and esxB are part of RD1 (part of a 15-gene locus known as ESX-1), a section of DNA deleted in the M.bovis BCG strain used for vaccination. Deletion of this region is thought to be largely responsible for the attenuation of BCG, and esxA and EsxB in particular are quite important in this effect (PubMed:14557547, PubMed:14756778, PubMed:16368961).3 Publications
Secretion of EspA, EsxA and EsxB is mutually dependent (PubMed:16030141).1 Publication
To improve expression in E.coli the proteins were cloned as a single protein in the order esxB-esxA with a cleavable thrombin tag (PubMed:19854905).1 Publication

<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 functionChaperone
Biological processVirulence

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-8172-MONOMER

<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:
ESAT-6-like protein EsxB
Alternative name(s):
10 kDa culture filtrate antigen CFP-101 Publication
Short name:
CFP-10
Secreted antigenic protein MTSA-10
<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:esxB1 Publication
Synonyms:cfp10, lhp1 Publication, mtsA101 Publication
Ordered Locus Names:Rv3874
ORF Names:MTV027.09
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<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
  • UP000001584 <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

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv3874

<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

Cell wall, Host endoplasmic reticulum, 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

Bacteria no longer translocate from the phagolysosome to the cytosol of host (human) cells probably due to polar effects on the downstream esxA gene; bacteria replicate in phagolysosome, decreased apoptosis of infected host (human) dendritic cells (PubMed:17604718). Loss of ability to lyse host (human) lung epithelial cells, possibly due to polar effects on the downstream esxA gene; in BALB/c-infected mice bacteria are not as invasive and cause decreased lung disease (PubMed:14557547). No growth in the human macrophage-like cell line THP-1, no cytotoxicity (PubMed:14756778). Inactivation leads to absence of EsxA and EsxB from cell lysates (PubMed:14756778, PubMed:16368961). No secretion of EspA (PubMed:16030141).4 Publications

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>Mutagenesisi42Q → P: Abolishes EsxB-EsxA heterodimer interaction with EccCb1 and EspA, maintains interaction with EccA2 and EccE2. 1 Publication1
Mutagenesisi62A → S: Abolishes EsxB-EsxA heterodimer interaction with EccCb1, weaker interaction with EspA, maintains interaction with EccA2 and EccE2. 1 Publication1
Mutagenesisi94L → A: Abolishes interaction with EccCb1, but not with EsxA. 1 Publication1
Mutagenesisi95S → T: Abolishes EsxB-EsxA heterodimer interaction with EccCb1, maintains interaction with EspA, EccA2 and EccE2. 1 Publication1
Mutagenesisi96S → A: No change in stability. 1 Publication1
Mutagenesisi98M → A: Abolishes interaction with EccCb1, but not with EsxA. No change in stability, but loss of secretion. 1 Publication1
Mutagenesisi99G → A: Abolishes interaction with EccCb1, but not with EsxA. 1 Publication1
Mutagenesisi100F → A: Abolishes interaction with EccCb1, but not with EsxA. No change in stability, but loss of secretion. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00001677962 – 100ESAT-6-like protein EsxBAdd BLAST99

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 residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P9WNK5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P9WNK5

<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

Constitutively expressed, part of the esxB-esxA operon (PubMed:9846755).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

Able to form a homodimer (By similarity).

Forms a tight 1:1 complex with EsxA (ESAT-6) (PubMed:11940590, PubMed:14557536, PubMed:16048998, PubMed:16973880, PubMed:19854905, PubMed:19906174, PubMed:23150662, PubMed:26260636, PubMed:20085764, PubMed:15973432, PubMed:24586681). The complex persists even after secretion (PubMed:16048998). In vitro EsxB only interacts with non-acetylated EsxA; it interacts with C-terminally truncated EsxA (missing the last 10 residues) (PubMed:15378760). The native EsxA-EsxB complex dissociates at pH 4.0, and EsxA may then be freed to then lyse membranes (PubMed:17557817). Another study using recombinant protein did not find dissociation at acidic pH (PubMed:23150662). Recombinant heterodimer (with a His tag on EsxB) can be dissociated by the detergents amidosulfobetaine-14 and lauryldimethylamine N-oxide (PubMed:26260636).

Interacts with EccCb1 (PubMed:14557536, PubMed:16973880, PubMed:25865481).

Interacts with PPE68 (PubMed:17433643).

Interacts with EccCa1, EccCb1, EsxA, EspI and EspJ (PubMed:19854905). An artificial EsxB-EsxA heterodimer interacts with EspA, EccB1, EccCa1, EccCb1, EspI, EspJ, EccA2 and EccE2; the latter 2 are from the adjacent ESX-2 locus (PubMed:19854905).

Interacts with host (human) beta-2-microglobulin (B2M) in complex with EsxA; only binds free B2M and not B2M in complex with HLA-I (PubMed:25356553).

By similarity15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P9WNK5, 13 interactors

Molecular INTeraction database

More...
MINTi
P9WNK5

STRING: functional protein association networks

More...
STRINGi
83332.Rv3874

<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

1100
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P9WNK5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni87 – 100Required for ESAT-6/CFP-10 complex to bind to host macrophage and monocytes1 PublicationAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili7 – 421 PublicationAdd BLAST36
Coiled coili49 – 86Sequence analysis1 PublicationAdd BLAST38

<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

May be secreted as a 4 coiled-coil complex with EsxA (PubMed:16048998). The C-terminal domain is required for interaction with both EsxA and EccCb1; the last 7 amino acids are necessary and sufficient for EccCb1 binding and secretion (PubMed:16973880).2 Publications

<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 WXG100 family. CFP-10 subfamily.1 Publication

Keywords - Domaini

Coiled coil

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
DISANIH

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036689 ESAT-6-like_sf
IPR010310 T7SS_ESAT-6-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06013 WXG100, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF140453 SSF140453, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03930 WXG100_ESAT6, 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>. 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_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.

P9WNK5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEMKTDAAT LAQEAGNFER ISGDLKTQID QVESTAGSLQ GQWRGAAGTA
60 70 80 90 100
AQAAVVRFQE AANKQKQELD EISTNIRQAG VQYSRADEEQ QQALSSQMGF
Length:100
Mass (Da):10,794
Last modified:April 16, 2014 - 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:i285F4FC96F55D194
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
AF004671 Genomic DNA Translation: AAC83445.1
AF419854 Genomic DNA Translation: AAL14999.1
AL123456 Genomic DNA Translation: CCP46703.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H70802

NCBI Reference Sequences

More...
RefSeqi
NP_218391.1, NC_000962.3
WP_003399940.1, NZ_NVQJ01000074.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP46703; CCP46703; Rv3874

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
886194

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv3874

<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
AF004671 Genomic DNA Translation: AAC83445.1
AF419854 Genomic DNA Translation: AAL14999.1
AL123456 Genomic DNA Translation: CCP46703.1
PIRiH70802
RefSeqiNP_218391.1, NC_000962.3
WP_003399940.1, NZ_NVQJ01000074.1

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
1WA8NMR-A2-100[»]
3FAVX-ray2.15A/C1-100[»]
SMRiP9WNK5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP9WNK5, 13 interactors
MINTiP9WNK5
STRINGi83332.Rv3874

PTM databases

iPTMnetiP9WNK5

Proteomic databases

PaxDbiP9WNK5

Genome annotation databases

EnsemblBacteriaiCCP46703; CCP46703; Rv3874
GeneIDi886194
KEGGimtu:Rv3874

Organism-specific databases

TubercuListiRv3874

Phylogenomic databases

OMAiDISANIH

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-8172-MONOMER

Family and domain databases

InterProiView protein in InterPro
IPR036689 ESAT-6-like_sf
IPR010310 T7SS_ESAT-6-like
PfamiView protein in Pfam
PF06013 WXG100, 1 hit
SUPFAMiSSF140453 SSF140453, 1 hit
TIGRFAMsiTIGR03930 WXG100_ESAT6, 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 nameiESXB_MYCTU
<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: P9WNK5
Secondary accession number(s): L0TDT9, O69739, P0A566
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: October 16, 2019
This is version 35 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. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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