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

Cell division protein FtsZ

Gene

ftsZ

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

Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei136GTPUniRule annotation2 Publications1
Binding sitei140GTPUniRule annotation2 Publications1
Binding sitei184GTPUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi18 – 22GTPUniRule annotation2 Publications5
Nucleotide bindingi105 – 107GTPUniRule annotation2 Publications3

<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 processCell cycle, Cell division, Septation
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-6358-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:
Cell division protein FtsZUniRule annotation
<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:ftsZUniRule annotation
Ordered Locus Names:Rv2150c
ORF Names:MTCY270.18
<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
Rv2150c

<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

Cytoplasm

<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

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>Mutagenesisi135F → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi137G → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi138K → A: Decrease in GTPase activity. 1 Publication1
Mutagenesisi164D → A: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi176L → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi179A → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi203L → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi204I → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi210D → G: Reduces FtsZ polymerization and GTP hydrolysis. Does not affect the structure or the stability of the unpolymerized FtsZ. 1 Publication1
Mutagenesisi269L → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi289I → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi291F → E: Strong decrease in GTPase activity. 1 Publication1
Mutagenesisi343T → A: Lack of phosphorylation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4213

Drug and drug target database

More...
DrugBanki
DB01864 5'-Guanosine-Diphosphate-Monothiophosphate
DB04272 Citric acid
DB04315 Guanosine-5'-Diphosphate

<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_00001143651 – 379Cell division protein FtsZAdd BLAST379

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 residuei343Phosphothreonine1 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

Phosphorylated by PknA. Phosphorylation is required for FtsZ-FhaB interaction.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P9WN95

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P9WN95

<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

Homodimer (PubMed:23888039). Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner.

Interacts directly with several other division proteins (By similarity).

Interacts with FhaB and FtsQ in a PknA-dependent manner. Initial interaction between FtsZ and FhaB is necessary for ternary FtsZ-FhaB-FtsQ complex formation.

UniRule annotation4 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

WithEntry#Exp.IntActNotes
P9WP575EBI-6414519,EBI-6414478

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P9WN95, 1 interactor

STRING: functional protein association networks

More...
STRINGi
83332.Rv2150c

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P9WN95

<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

1379
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
P9WN95

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

<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 FtsZ family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CDK Bacteria
COG0206 LUCA

KEGG Orthology (KO)

More...
KOi
K03531

Identification of Orthologs from Complete Genome Data

More...
OMAi
GRRRANQ

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WN95

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02201 FtsZ_type1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00909 FtsZ, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000158 Cell_div_FtsZ
IPR020805 Cell_div_FtsZ_CS
IPR024757 FtsZ_C
IPR008280 Tub_FtsZ_C
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR003008 Tubulin_FtsZ_GTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12327 FtsZ_C, 1 hit
PF00091 Tubulin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00423 CELLDVISFTSZ

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00065 ftsZ, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01134 FTSZ_1, 1 hit
PS01135 FTSZ_2, 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.

P9WN95-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPPHNYLAV IKVVGIGGGG VNAVNRMIEQ GLKGVEFIAI NTDAQALLMS
60 70 80 90 100
DADVKLDVGR DSTRGLGAGA DPEVGRKAAE DAKDEIEELL RGADMVFVTA
110 120 130 140 150
GEGGGTGTGG APVVASIARK LGALTVGVVT RPFSFEGKRR SNQAENGIAA
160 170 180 190 200
LRESCDTLIV IPNDRLLQMG DAAVSLMDAF RSADEVLLNG VQGITDLITT
210 220 230 240 250
PGLINVDFAD VKGIMSGAGT ALMGIGSARG EGRSLKAAEI AINSPLLEAS
260 270 280 290 300
MEGAQGVLMS IAGGSDLGLF EINEAASLVQ DAAHPDANII FGTVIDDSLG
310 320 330 340 350
DEVRVTVIAA GFDVSGPGRK PVMGETGGAH RIESAKAGKL TSTLFEPVDA
360 370
VSVPLHTNGA TLSIGGDDDD VDVPPFMRR
Length:379
Mass (Da):38,756
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:i3F580353078788A9
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: CCP44926.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B70579

NCBI Reference Sequences

More...
RefSeqi
NP_216666.1, NC_000962.3
WP_003411144.1, NZ_NVQJ01000044.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP44926; CCP44926; Rv2150c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
888369

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2150c
mtv:RVBD_2150c

<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: CCP44926.1
PIRiB70579
RefSeqiNP_216666.1, NC_000962.3
WP_003411144.1, NZ_NVQJ01000044.1

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
1RLUX-ray2.08A/B1-379[»]
1RQ2X-ray1.86A/B1-379[»]
1RQ7X-ray2.60A/B1-379[»]
2Q1XX-ray2.35A/B1-379[»]
2Q1YX-ray2.30A/B1-379[»]
4KWEX-ray2.91A/B/C1-379[»]
5V68X-ray3.46A/B/C/D/E/F1-379[»]
5ZUEX-ray2.70A1-379[»]
SMRiP9WN95
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP9WN95, 1 interactor
STRINGi83332.Rv2150c

Chemistry databases

BindingDBiP9WN95
ChEMBLiCHEMBL4213
DrugBankiDB01864 5'-Guanosine-Diphosphate-Monothiophosphate
DB04272 Citric acid
DB04315 Guanosine-5'-Diphosphate

PTM databases

iPTMnetiP9WN95

Proteomic databases

PaxDbiP9WN95

Genome annotation databases

EnsemblBacteriaiCCP44926; CCP44926; Rv2150c
GeneIDi888369
KEGGimtu:Rv2150c
mtv:RVBD_2150c

Organism-specific databases

TubercuListiRv2150c

Phylogenomic databases

eggNOGiENOG4105CDK Bacteria
COG0206 LUCA
KOiK03531
OMAiGRRRANQ
PhylomeDBiP9WN95

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6358-MONOMER

Family and domain databases

CDDicd02201 FtsZ_type1, 1 hit
Gene3Di3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
HAMAPiMF_00909 FtsZ, 1 hit
InterProiView protein in InterPro
IPR000158 Cell_div_FtsZ
IPR020805 Cell_div_FtsZ_CS
IPR024757 FtsZ_C
IPR008280 Tub_FtsZ_C
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR003008 Tubulin_FtsZ_GTPase
PfamiView protein in Pfam
PF12327 FtsZ_C, 1 hit
PF00091 Tubulin, 1 hit
PRINTSiPR00423 CELLDVISFTSZ
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
TIGRFAMsiTIGR00065 ftsZ, 1 hit
PROSITEiView protein in PROSITE
PS01134 FTSZ_1, 1 hit
PS01135 FTSZ_2, 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 nameiFTSZ_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: P9WN95
Secondary accession number(s): L0TBN4, O08378, P64170
<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, 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