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Entry version 155 (16 Oct 2019)
Sequence version 3 (16 Jun 2009)
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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Bacillus subtilis (strain 168)
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 annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

During sporulation, is negatively regulated by MciZ, which binds to FtsZ and inhibits its polymerization and the formation of the Z ring.2 Publications

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 sitei139GTPUniRule annotation1 Publication1
Binding sitei143GTPUniRule annotation1 Publication1
Binding sitei187GTPUniRule annotation1 Publication1

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 bindingi21 – 25GTPUniRule annotation1 Publication5
Nucleotide bindingi108 – 110GTPUniRule annotation1 Publication3

<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
BSUB:BSU15290-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:BSU15290
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<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>Mutagenesisi280D → R: Disrupts interaction with MciZ. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5690

<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_00001143411 – 382Cell division protein FtsZAdd BLAST382

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P17865

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

More...
PaxDbi
P17865

PRoteomics IDEntifications database

More...
PRIDEi
P17865

<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. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity).

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

Interacts with FtsA (PubMed:16159787).

Interacts with Phi29 DNA replication protein 1 (PubMed:23836667).

Interacts with the cell division inhibitor MciZ (PubMed:23836667, PubMed:25848052).

UniRule annotation3 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

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P17865, 9 interactors

Molecular INTeraction database

More...
MINTi
P17865

STRING: functional protein association networks

More...
STRINGi
224308.BSU15290

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P17865

<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

1382
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
P17865

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P17865

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000049094

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17865

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
P17865

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.

P17865-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLEFETNIDG LASIKVIGVG GGGNNAVNRM IENEVQGVEY IAVNTDAQAL
60 70 80 90 100
NLSKAEVKMQ IGAKLTRGLG AGANPEVGKK AAEESKEQIE EALKGADMVF
110 120 130 140 150
VTAGMGGGTG TGAAPVIAQI AKDLGALTVG VVTRPFTFEG RKRQLQAAGG
160 170 180 190 200
ISAMKEAVDT LIVIPNDRIL EIVDKNTPML EAFREADNVL RQGVQGISDL
210 220 230 240 250
IATPGLINLD FADVKTIMSN KGSALMGIGI ATGENRAAEA AKKAISSPLL
260 270 280 290 300
EAAIDGAQGV LMNITGGTNL SLYEVQEAAD IVASASDQDV NMIFGSVINE
310 320 330 340 350
NLKDEIVVTV IATGFIEQEK DVTKPQRPSL NQSIKTHNQS VPKREPKREE
360 370 380
PQQQNTVSRH TSQPADDTLD IPTFLRNRNK RG
Length:382
Mass (Da):40,395
Last modified:June 16, 2009 - v3
<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:i24E908DEC9685614
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti345 – 346EP → DA in AAA22457 (PubMed:3139638).Curated2

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
M22630 Genomic DNA Translation: AAA22457.1
AL009126 Genomic DNA Translation: CAB13402.2
J05400 Genomic DNA Translation: AAA83361.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I39848

NCBI Reference Sequences

More...
RefSeqi
NP_389412.2, NC_000964.3
WP_003232167.1, NZ_JNCM01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB13402; CAB13402; BSU15290

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
935971

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU15290

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.1667

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

Becoming two - Issue 171 of July 2015

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22630 Genomic DNA Translation: AAA22457.1
AL009126 Genomic DNA Translation: CAB13402.2
J05400 Genomic DNA Translation: AAA83361.1
PIRiI39848
RefSeqiNP_389412.2, NC_000964.3
WP_003232167.1, NZ_JNCM01000035.1

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
2RHHX-ray2.00A12-315[»]
2RHJX-ray1.76A12-315[»]
2RHLX-ray2.45A/B12-315[»]
2RHOX-ray2.45A/B12-315[»]
2VAMX-ray2.50A1-382[»]
2VXYX-ray1.70A1-382[»]
4U39X-ray3.19A/B/C/D/E/F/G/H/I12-315[»]
SMRiP17865
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP17865, 9 interactors
MINTiP17865
STRINGi224308.BSU15290

Chemistry databases

BindingDBiP17865
ChEMBLiCHEMBL5690

Proteomic databases

jPOSTiP17865
PaxDbiP17865
PRIDEiP17865

Genome annotation databases

EnsemblBacteriaiCAB13402; CAB13402; BSU15290
GeneIDi935971
KEGGibsu:BSU15290
PATRICifig|224308.179.peg.1667

Phylogenomic databases

eggNOGiENOG4105CDK Bacteria
COG0206 LUCA
HOGENOMiHOG000049094
InParanoidiP17865
KOiK03531
OMAiGRRRANQ
PhylomeDBiP17865

Enzyme and pathway databases

BioCyciBSUB:BSU15290-MONOMER

Miscellaneous databases

EvolutionaryTraceiP17865

Protein Ontology

More...
PROi
PR:P17865

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_BACSU
<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: P17865
<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 1, 1990
Last sequence update: June 16, 2009
Last modified: October 16, 2019
This is version 155 of the entry and version 3 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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