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Entry version 137 (12 Aug 2020)
Sequence version 1 (19 Jul 2005)
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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Escherichia coli (strain K12)
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. Polymerization and bundle formation is enhanced by CbeA.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Formation of the FtsZ ring is inhibited by SulA, MinCD, DicB and toxins CbtA and CptA. Inhibition by toxin CbtA, SulA or DicB overexpression is neutralized by cytoskeleton bundling-enhancing protein CbeA, while inhibition by toxin CptA is neutralized by antitoxin CptB (PubMed:21166897, PubMed:22239607, PubMed:22515815, PubMed:8752322). Either FtsA or ZipA is required for Z ring formation and stabilization (PubMed:11847116).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei138GTPUniRule annotation1
Binding sitei142GTPUniRule annotation1
Binding sitei186GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi20 – 24GTPUniRule annotation5
Nucleotide bindingi107 – 109GTPUniRule annotation3

<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
EcoCyc:EG10347-MONOMER
ECOL316407:JW0093-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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
Synonyms:sfiB, sulB
Ordered Locus Names:b0095, JW0093
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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
  • UP000000625 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1 – 32Missing : No interaction with MreB or CbtA (YeeV). 1 PublicationAdd BLAST32
Mutagenesisi33 – 49Missing : No interaction with CtpA. Add BLAST17
Mutagenesisi105G → S in FtsZ-84; loss of GTPase-activity and conversion to an ATPase. 1 Publication1
Mutagenesisi108T → A in FtsZ-Z3; lethal; greatly reduced GTP binding. 1
Mutagenesisi174R → D: Protein has decreased affinity for the cell inner membrane, polymerizes into filaments less efficiently than wild-type, the protofilaments no longer form bundles, still forms rings. 1 Publication1
Mutagenesisi317 – 383Missing : No interaction with MreB or CbtA (YeeV). 1 PublicationAdd BLAST67

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3999

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001143491 – 383Cell division protein FtsZAdd BLAST383

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 residuei174(Microbial infection) ADP-ribosylarginine; by S.proteamaculans Tre11 Publication1
Modified residuei338(Microbial infection) ADP-ribosylarginine; by S.proteamaculans Tre11 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

(Microbial infection) ADP-ribosylated on Arg-174 and sometimes Arg-338 by Tre1 when infected by S.proteamaculans strain 568. This prevents the formation of Z rings, inhibiting cell division, leading to cell elongation and disadvantaging E.coli over S.proteamaculans during competition for nutrients. In vitro it can be de-ADP-ribosylated by S.proteamaculans Tri1.1 Publication

Keywords - PTMi

ADP-ribosylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9A6

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

More...
PaxDbi
P0A9A6

PRoteomics IDEntifications database

More...
PRIDEi
P0A9A6

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A9A6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Repressed 1.3-fold by hydroxyurea (at protein level).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'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%5Fsection">'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. Polymers persist as long as GTP is present and disappear rapidly as soon as it is consumed.

Interacts directly with several other division proteins, including FtsA and ZipA.

Interacts with polymerization inhibitors SulA, CbtA and CptA.

Interacts with MreB and polymerization bundling-enhancing factor CbeA.

Interacts with CbtA, YkfI and YpjF (PubMed:28257056).

14 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261887, 577 interactors
849188, 8 interactors

Database of interacting proteins

More...
DIPi
DIP-31873N

Protein interaction database and analysis system

More...
IntActi
P0A9A6, 61 interactors

Molecular INTeraction database

More...
MINTi
P0A9A6

STRING: functional protein association networks

More...
STRINGi
511145.b0095

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A9A6

<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

1383
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
P0A9A6

Database of comparative protein structure models

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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
P0A9A6

<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 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

The central and C-terminal regions are required for dimerization.1 Publication

<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
COG0206, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_024865_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9A6

KEGG Orthology (KO)

More...
KOi
K03531

Database for complete collections of gene phylogenies

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PhylomeDBi
P0A9A6

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02201, FtsZ_type1, 1 hit

Database of protein disorder

More...
DisProti
DP02201

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0A9A6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR
60 70 80 90 100
KTAVGQTIQI GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI
110 120 130 140 150
AAGMGGGTGT GAAPVVAEVA KDLGILTVAV VTKPFNFEGK KRMAFAEQGI
160 170 180 190 200
TELSKHVDSL ITIPNDKLLK VLGRGISLLD AFGAANDVLK GAVQGIAELI
210 220 230 240 250
TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA EMAISSPLLE
260 270 280 290 300
DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP
310 320 330 340 350
DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE
360 370 380
QKPVAKVVND NAPQTAKEPD YLDIPAFLRK QAD
Length:383
Mass (Da):40,324
Last modified:July 19, 2005 - 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:iB3A53340367DBBA0
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 conflicti32 – 39ERIEGVEF → DALKVLNS in AAA23818 (PubMed:6094474).Curated8
Sequence conflicti158D → N in CAA38872 (PubMed:3000876).Curated1
Sequence conflicti222Y → H in CAA38872 (PubMed:3000876).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73206.1
AP009048 Genomic DNA Translation: BAB96663.2
X55034 Genomic DNA Translation: CAA38872.1
K02668 Genomic DNA Translation: AAA23818.1
M19211 Genomic DNA Translation: AAA83848.1

Protein sequence database of the Protein Information Resource

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PIRi
G64731, CEECZ

NCBI Reference Sequences

More...
RefSeqi
NP_414637.1, NC_000913.3
WP_000462776.1, NZ_STEB01000010.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73206; AAC73206; b0095
BAB96663; BAB96663; BAB96663

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
49586092
944786

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0093
eco:b0095

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2185

<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%5Freferences%5Fsection">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
U00096 Genomic DNA Translation: AAC73206.1
AP009048 Genomic DNA Translation: BAB96663.2
X55034 Genomic DNA Translation: CAA38872.1
K02668 Genomic DNA Translation: AAA23818.1
M19211 Genomic DNA Translation: AAA83848.1
PIRiG64731, CEECZ
RefSeqiNP_414637.1, NC_000913.3
WP_000462776.1, NZ_STEB01000010.1

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
1F47X-ray1.95A367-383[»]
5HAWX-ray1.89K/L370-379[»]
5HBUX-ray2.60K370-379[»]
5HSZX-ray2.30K372-382[»]
5K58X-ray2.77K/L/M/N372-379[»]
5KOAX-ray2.67D370-381[»]
SMRiP0A9A6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261887, 577 interactors
849188, 8 interactors
DIPiDIP-31873N
IntActiP0A9A6, 61 interactors
MINTiP0A9A6
STRINGi511145.b0095

Chemistry databases

BindingDBiP0A9A6
ChEMBLiCHEMBL3999

2D gel databases

SWISS-2DPAGEiP0A9A6

Proteomic databases

jPOSTiP0A9A6
PaxDbiP0A9A6
PRIDEiP0A9A6

Genome annotation databases

EnsemblBacteriaiAAC73206; AAC73206; b0095
BAB96663; BAB96663; BAB96663
GeneIDi49586092
944786
KEGGiecj:JW0093
eco:b0095
PATRICifig|1411691.4.peg.2185

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0343

Phylogenomic databases

eggNOGiCOG0206, Bacteria
HOGENOMiCLU_024865_0_1_6
InParanoidiP0A9A6
KOiK03531
PhylomeDBiP0A9A6

Enzyme and pathway databases

BioCyciEcoCyc:EG10347-MONOMER
ECOL316407:JW0093-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A9A6

Protein Ontology

More...
PROi
PR:P0A9A6

Family and domain databases

CDDicd02201, FtsZ_type1, 1 hit
DisProtiDP02201
Gene3Di3.40.50.1440, 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
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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_ECOLI
<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: P0A9A6
Secondary accession number(s): P06138, P77857, P78047
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 19, 2005
Last modified: August 12, 2020
This is version 137 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, Direct protein sequencing, 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
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