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Entry version 37 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Lipoarabinomannan carrier protein LprG

Gene

lprG

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

Probably helps membrane protein Rv1410c (P55) transport triacylglycerides (TAG) across the inner cell membrane into the periplasm; TAG probably regulates lipid metabolism and growth regulation (PubMed:26751071). Binds TAG and transfers it between lipid bilayers, probably to the outer membrane in vivo (PubMed:26751071). Binds di- and triacylated phosphatidyl-myo-inositol mannosides (PIMs), and glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM), facilitating their recognition by TLR2 (PubMed:20694006, PubMed:25356793). Binds LM > PIM6 > ManLAM > PI-LAM > PIM2 (mannose-capped LAM and phospho-myo-inositol-capped LAM, E.coli expressed without acyl-groups); deacylated LM and LAM also bind to this protein via their mannose moieties, showing LprG has at least 2 different ways to bind glycolipids (PubMed:25356793). Binds triacylglycerides (TAG) in the same cavity, is able to transfer TAG between lipid bilayers (PubMed:26751071). Overexpression of LprG and Rv1410c leads to increased levels of TAG in the culture medium (PubMed:26751071). Required for Rv1410c-mediated export of drugs (PubMed:18156250, PubMed:21762531). Required, probably with Rv1410c, for normal surface localization of LAM (PubMed:25232742).6 Publications
A host TLR2 agonist (toll-like receptor), shown experimentally for human and mouse (PubMed:19362712). Inhibits primary human macrophage MHC-II Ag processing via TLR2 (PubMed:15294983). Both lipidated and nonlipidated protein act as TLR2 agonists in antigen-presenting cells, although lipidated protein is more efficient (PubMed:20694006). In resting human CD4+ T-cells lipidated but not nonlipidated protein is a costimulatory ligand (with anti-CD3 and anti-CD28) for T-cell proliferation and IFN-gamma and IL-2 production, leading to increased expression of early T-cell activation markers, TLR2 and NFKB3 phosphorylation (PubMed:21078852). Human CD4+ T-cells use TLR1/TLR2 heterodimers to respond to this and probably other mycobacterial lipoproteins (PubMed:21078852). Able to stimulate proliferation of CD4+ T-cells derived from a human leprosy patient following protein processing/presentation by MHC class II molecules in peripheral blood mononuclear cells (PubMed:18424702). Requires both host TLR1 and TLR2 as coreceptors to elicit host response in mouse, although TLR6 may play a redundant role, has a partial requirement for CD14 as an accessory receptor (PubMed:19362712).5 Publications

Miscellaneous

Bacterial LAM blocks host cell phagosome-lysosome fusion and is one way in which M.tuberculosis evades the host immune system.2 Publications
Triacylglycerides accumulate in lipid droplets in the cytoplasm of M.tuberculosis stationary phase and dormant bacteria, and are used as an energy source during starvation (PubMed:26751071).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

Biological processAntibiotic resistance, Lipid transport, Transport, Virulence
LigandLipid-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-5594-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:
Lipoarabinomannan carrier protein LprG2 Publications
Alternative name(s):
27 kDa lipoprotein
Antigen P271 Publication
Lipoprotein LprG
Triacylated glycolipid carrier LprG1 Publication
Triacylglyceride transfer protein LprG1 Publication
<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:lprG
Synonyms:lpp-27
Ordered Locus Names:Rv1411c
ORF Names:MTCY21B4.28c
<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
Rv1411c

<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 inner membrane, Cell membrane, Cell wall, Membrane, 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 deletion mutant leads to loss of expression of efflux pump Rv1410c due to polar effects; in infected BALB/c mice 1.5 and 2.5 log decrease in bacterial load 15 and 35 days after infection (PubMed:14998516). The single mutant increases sensitivity to malachite green, sodium dodecyl sulfate (SDS), isoniazid, ethambutal and ethidium bromide, alters the permeability of the cell wall; both genes of the operon are required to fully restore the phenotypes (PubMed:21762531). Single deletion mutant (probably without Rv1410c) has decreased surface-exposed glycolipid lipoarabinomannan (LAM), although cellular LAM, LM and PIM content is normal (PubMed:25232742, PubMed:25356793). Disruption of either Rv1410c or the lrpG-Rv1410c operon leads to increased levels of many triacylglyceride (TAG) alkylforms; up to 100-fold increase depending on the exact TAG form (PubMed:26751071). It also forms smaller colonies on agar (PubMed:25232742). Loss of surface LAM has several consequences; bacteria enter mouse macrophages with reduced efficiency and block mouse macrophage phagosome-lysosome fusion less efficiently than wild-type (PubMed:25232742). Reduced efficiency of mouse macrophage phagosome-lysosome fusion was seen in another study (PubMed:25356793). C57BL/6 mice infected with mutant bacteria have 10-fold less bacterial burden after 10 days and about 2700-fold less burden after 70 days; attenuation of mutant is not rescued in macrophages impaired for reactive oxygen or nitrogen generation (disruption of Ncf1 or iNOS) (PubMed:25232742).5 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>Mutagenesisi91V → W: Decreased TLR2 agonist activity, cannot acquire lipid from mycobacterial extracts, cavity entrance and size decrease. Binds PIM6, LM and ManLAM 10-100-fold less well than wild-type, binds de-acylated LM and ManLAM as well as wild-type. Decreased ability to transfer triacylglyceride between lipid bilayers. 3 Publications1

<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 – 26PROSITE-ProRule annotationAdd BLAST26
<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_000001814627 – 236Lipoarabinomannan carrier protein LprGPROSITE-ProRule annotationAdd BLAST210

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi27N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication1
Lipidationi27S-diacylglycerol cysteinePROSITE-ProRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Modified by Lgt on Cys-27 with an S-linked diacylglyceral, signal peptide is removed by LspA, Cys-27 is further modifed with a fatty acid on its amino group by Lnt yielding a triacylated protein (Probable). Probably glycosylated, which is required for T-cell activation (PubMed:18424702).By similarity1 Publication1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

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

More...
PaxDbi
P9WK45

<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
83332.Rv1411c

<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

1236
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
P9WK45

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>Regioni81 – 100Prevents bacterial uptake by a human macrophage-like cell line1 PublicationAdd BLAST20
Regioni141 – 160Prevents bacterial uptake by a human macrophage-like cell line1 PublicationAdd BLAST20
Regioni218 – 236Prevents bacterial uptake by a human macrophage-like cell line1 PublicationAdd BLAST19

<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

Forms a U-shaped beta-half-barrel with a small hydrophobic cavity (1500 Angstroms (3)) which holds a triacylated PIM in 1 crystal structure; the 3 acyl chains are within the cavity while the sugar moieties bind to the protein surface (PubMed:20694006). In the structure bound to triacylglycerides (TAG) 2 of the 3 acyl chains are buried in the cavity, the third is solvent exposed (PubMed:26751071). A flexible lid region may move to accommodate different TAG molecules (PubMed:26751071). Fragments of the mature protein (residues 81-100, 141-160 and 218-236) prevent uptake of M.tuberculosis by a human macrophage-like cell line; lesser effects are seen on bacterial uptake by a human lung epithelial cell line (PubMed:25041568).3 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 LppX/LprAFG lipoprotein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG41064B9 Bacteria
ENOG4112A10 LUCA

KEGG Orthology (KO)

More...
KOi
K14954

Identification of Orthologs from Complete Genome Data

More...
OMAi
TLTPNKW

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WK45

Family and domain databases

Conserved Domains Database

More...
CDDi
cd16334 LppX-like, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029046 LolA/LolB/LppX
IPR009830 LppX/LprAFG

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07161 LppX_LprAFG, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF89392 SSF89392, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 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.

P9WK45-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRTPRRHCRR IAVLAAVSIA ATVVAGCSSG SKPSGGPLPD AKPLVEEATA
60 70 80 90 100
QTKALKSAHM VLTVNGKIPG LSLKTLSGDL TTNPTAATGN VKLTLGGSDI
110 120 130 140 150
DADFVVFDGI LYATLTPNQW SDFGPAADIY DPAQVLNPDT GLANVLANFA
160 170 180 190 200
DAKAEGRDTI NGQNTIRISG KVSAQAVNQI APPFNATQPV PATVWIQETG
210 220 230
DHQLAQAQLD RGSGNSVQMT LSKWGEKVQV TKPPVS
Length:236
Mass (Da):24,548
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:i2591DAE6D2E2DC22
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
AL123456 Genomic DNA Translation: CCP44170.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H70901

NCBI Reference Sequences

More...
RefSeqi
NP_215927.1, NC_000962.3
WP_003407315.1, NZ_NVQJ01000038.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP44170; CCP44170; Rv1411c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
886700

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv1411c
mtv:RVBD_1411c

<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
AL123456 Genomic DNA Translation: CCP44170.1
PIRiH70901
RefSeqiNP_215927.1, NC_000962.3
WP_003407315.1, NZ_NVQJ01000038.1

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
3MH8X-ray2.00A/B36-231[»]
3MH9X-ray1.79A/C28-236[»]
3MHAX-ray1.85A/B36-231[»]
4ZRAX-ray1.83A/C36-231[»]
SMRiP9WK45
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1411c

Proteomic databases

PaxDbiP9WK45

Genome annotation databases

EnsemblBacteriaiCCP44170; CCP44170; Rv1411c
GeneIDi886700
KEGGimtu:Rv1411c
mtv:RVBD_1411c

Organism-specific databases

TubercuListiRv1411c

Phylogenomic databases

eggNOGiENOG41064B9 Bacteria
ENOG4112A10 LUCA
KOiK14954
OMAiTLTPNKW
PhylomeDBiP9WK45

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5594-MONOMER

Family and domain databases

CDDicd16334 LppX-like, 1 hit
InterProiView protein in InterPro
IPR029046 LolA/LolB/LppX
IPR009830 LppX/LprAFG
PfamiView protein in Pfam
PF07161 LppX_LprAFG, 1 hit
SUPFAMiSSF89392 SSF89392, 1 hit
PROSITEiView protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 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 nameiLPRG_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: P9WK45
Secondary accession number(s): L0T868
, O32852, P0A5I8, P71679
<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: September 18, 2019
This is version 37 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, 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
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