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 131 (18 Sep 2019)
Sequence version 1 (01 Jun 1998)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase

Gene

ppm1

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

Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.1 Publication
Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can be modified, tested with the C-terminal domain expressed in M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM).1 Publication

Miscellaneous

In a number of other Mycobacteria, including M.avis, M.leprae and M.smegmatis, these domains are encoded by 2 separate adjacent genes.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lipoprotein biosynthesis (N-acyl transfer)

This protein is involved in the pathway lipoprotein biosynthesis (N-acyl transfer), which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway lipoprotein biosynthesis (N-acyl transfer) and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei294Proton acceptorPROSITE-ProRule annotation1
Active sitei359PROSITE-ProRule annotation1
Active sitei409NucleophilePROSITE-ProRule annotation1

<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 functionAcyltransferase, Glycosyltransferase, Hydrolase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G185E-6255-MONOMER
MTBH37RV:G185E-6255-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00666

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT2 Glycosyltransferase Family 2

<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:
Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
Including the following 2 domains:
Apolipoprotein N-acyltransferase1 Publication (EC:2.3.1.2691 Publication)
Short name:
ALP N-acyltransferaseBy similarity
Polyprenol monophosphomannose synthase1 Publication (EC:2.4.1.-1 Publication)
Short name:
PPM synthase1 Publication
Short name:
Polyprenol-P-Man synthase1 Publication
Short name:
Ppm11 Publication
Alternative name(s):
Dolichol-phosphate mannose synthase (EC:2.4.1.831 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:ppm11 Publication
Synonyms:lnt1 Publication
Ordered Locus Names:Rv2051c
<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
Rv2051c

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 22CytoplasmicBy similarityAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei23 – 42HelicalBy similarityAdd BLAST20
Topological domaini43 – 71ExtracellularBy similarityAdd BLAST29
Transmembranei72 – 89HelicalBy similarityAdd BLAST18
Topological domaini90 – 93CytoplasmicBy similarity4
Transmembranei94 – 115HelicalBy similarityAdd BLAST22
Topological domaini116 – 176ExtracellularBy similarityAdd BLAST61
Transmembranei177 – 194HelicalBy similarityAdd BLAST18
Topological domaini195 – 205CytoplasmicBy similarityAdd BLAST11
Transmembranei206 – 223HelicalBy similarityAdd BLAST18
Topological domaini224 – 508Extracellular1 PublicationAdd BLAST285
Transmembranei509 – 526HelicalBy similarityAdd BLAST18
Topological domaini527 – 874Cytoplasmic1 PublicationAdd BLAST348

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004345821 – 874Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthaseAdd BLAST874

Proteomic databases

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

More...
PaxDbi
O53493

PRoteomics IDEntifications database

More...
PRIDEi
O53493

<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.Rv2051c

<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

3D structure databases

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

More...
SMRi
O53493

Database of comparative protein structure models

More...
ModBasei
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini241 – 497CN hydrolasePROSITE-ProRule annotationAdd BLAST257

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>Regioni1 – 593Apolipoprotein N-acyltransferaseAdd BLAST593
Regioni594 – 874Polyprenol monophosphomannose synthase1 PublicationAdd BLAST281

<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

Consists of 2 domains; the N-terminus (residues 1-593) probably has the N-acyltransferase activity while the C-terminus (residues 594-874) has polyprenol monophosphomannose (PPM) synthase activity. The whole protein has higher PPM synthase than the second domain alone when expressed in M.smegmatis, suggesting the N-acyltransferase domain plays a stimulating role in PPM synthesis.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

In the N-terminal section; belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
In the C-terminal section; belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107R05 Bacteria
COG0815 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000021324

KEGG Orthology (KO)

More...
KOi
K03820

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADEMPND

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07571 ALP_N-acyl_transferase, 1 hit
cd06442 DPM1_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.110.10, 1 hit
3.90.550.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01148 Lnt, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004563 Apolipo_AcylTrfase
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
IPR039528 DPM1-like
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans

The PANTHER Classification System

More...
PANTHERi
PTHR43398 PTHR43398, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00795 CN_hydrolase, 1 hit
PF00535 Glycos_transf_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53448 SSF53448, 1 hit
SSF56317 SSF56317, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00546 lnt, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50263 CN_HYDROLASE, 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.

O53493-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLGAWVAAQ LPTTRTAVRT RLTRLVVSIV AGLLLYASFP PRNCWWAAVV
60 70 80 90 100
ALALLAWVLT HRATTPVGGL GYGLLFGLVF YVSLLPWIGE LVGPGPWLAL
110 120 130 140 150
ATTCALFPGI FGLFAVVVRL LPGWPIWFAV GWAAQEWLKS ILPFGGFPWG
160 170 180 190 200
SVAFGQAEGP LLPLVQLGGV ALLSTGVALV GCGLTAIALE IEKWWRTGGQ
210 220 230 240 250
GDAPPAVVLP AACICLVLFA AIVVWPQVRH AGSGSGGEPT VTVAVVQGNV
260 270 280 290 300
PRLGLDFNAQ RRAVLDNHVE ETLRLAADVH AGLAQQPQFV IWPENSSDID
310 320 330 340 350
PFVNPDAGQR ISAAAEAIGA PILIGTLMDV PGRPRENPEW TNTAIVWNPG
360 370 380 390 400
TGPADRHDKA IVQPFGEYLP MPWLFRHLSG YADRAGHFVP GNGTGVVRIA
410 420 430 440 450
GVPVGVATCW EVIFDRAPRK SILGGAQLLT VPSNNATFNK TMSEQQLAFA
460 470 480 490 500
KVRAVEHDRY VVVAGTTGIS AVIAPDGGEL IRTDFFQPAY LDSQVRLKTR
510 520 530 540 550
LTPATRWGPI LQWILVGAAA AVVLVAMRQN GWFPRPRRSE PKGENDDSDA
560 570 580 590 600
PPGRSEASGP PALSESDDEL IQPEQGGRHS SGFGRHRATS RSYMTTGQPA
610 620 630 640 650
PPAPGNRPSQ RVLVIIPTFN ERENLPVIHR RLTQACPAVH VLVVDDSSPD
660 670 680 690 700
GTGQLADELA QADPGRTHVM HRTAKNGLGA AYLAGFAWGL SREYSVLVEM
710 720 730 740 750
DADGSHAPEQ LQRLLDAVDA GADLAIGSRY VAGGTVRNWP WRRLVLSKTA
760 770 780 790 800
NTYSRLALGI GIHDITAGYR AYRREALEAI DLDGVDSKGY CFQIDLTWRT
810 820 830 840 850
VSNGFVVTEV PITFTERELG VSKMSGSNIR EALVKVARWG IEGRLSRSDH
860 870
ARARPDIARP GAGGSRVSRA DVTE
Length:874
Mass (Da):93,824
Last modified:June 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE00EADD2EC3238B4
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: CCP44824.1

NCBI Reference Sequences

More...
RefSeqi
NP_216567.1, NC_000962.3
WP_003902238.1, NZ_NVQJ01000047.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP44824; CCP44824; Rv2051c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
887402

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2051c
mtv:RVBD_2051c

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|83332.111.peg.2287

<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: CCP44824.1
RefSeqiNP_216567.1, NC_000962.3
WP_003902238.1, NZ_NVQJ01000047.1

3D structure databases

SMRiO53493
ModBaseiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2051c

Protein family/group databases

CAZyiGT2 Glycosyltransferase Family 2

Proteomic databases

PaxDbiO53493
PRIDEiO53493

Genome annotation databases

EnsemblBacteriaiCCP44824; CCP44824; Rv2051c
GeneIDi887402
KEGGimtu:Rv2051c
mtv:RVBD_2051c
PATRICifig|83332.111.peg.2287

Organism-specific databases

TubercuListiRv2051c

Phylogenomic databases

eggNOGiENOG4107R05 Bacteria
COG0815 LUCA
HOGENOMiHOG000021324
KOiK03820
OMAiADEMPND

Enzyme and pathway databases

UniPathwayiUPA00666
BioCyciMetaCyc:G185E-6255-MONOMER
MTBH37RV:G185E-6255-MONOMER

Family and domain databases

CDDicd07571 ALP_N-acyl_transferase, 1 hit
cd06442 DPM1_like, 1 hit
Gene3Di3.60.110.10, 1 hit
3.90.550.10, 1 hit
HAMAPiMF_01148 Lnt, 1 hit
InterProiView protein in InterPro
IPR004563 Apolipo_AcylTrfase
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
IPR039528 DPM1-like
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR43398 PTHR43398, 1 hit
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
PF00535 Glycos_transf_2, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
SSF56317 SSF56317, 1 hit
TIGRFAMsiTIGR00546 lnt, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 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 nameiPPMNT_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: O53493
Secondary accession number(s): F2GDY6, I6Y888, L0TBC5
<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: November 11, 2015
Last sequence update: June 1, 1998
Last modified: September 18, 2019
This is version 131 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

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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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