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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361GTPUniRule annotation
Binding sitei140 – 1401GTPUniRule annotation
Binding sitei184 – 1841GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225GTPUniRule annotation
Nucleotide bindingi105 – 1073GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:ML0917
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0917.

Subcellular locationi

  • Cytoplasm UniRule annotation

  • Note: Assembles at midcell at the inner surface of the cytoplasmic membrane.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Cell division protein FtsZPRO_0000114364Add
BLAST

Interactioni

Subunit structurei

Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins.UniRule annotation

Protein-protein interaction databases

STRINGi272631.ML0917.

Structurei

3D structure databases

ProteinModelPortaliQ9CCE4.
SMRiQ9CCE4. Positions 22-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiAQVIWGI.
OrthoDBiPOG091H02KK.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ. 1 hit.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CCE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPPHNYLAV IKVVGIGGGG VNAVNRMIEQ GLKGVEFMAI NTDAQALLMS
60 70 80 90 100
DADVKLDVGR DSTRGLGAGA DPEVGRKAAE DAKDEIEELL RGADMVFVTA
110 120 130 140 150
GEGGGTGTGG APVIASIARK LGALTVGVVT RPFSFEGKRR SNQAENGIAA
160 170 180 190 200
LRESCDTLIV IPNDRLLQMG DTAVSLMDAF RSADEVLLNG VQGITDLITT
210 220 230 240 250
PGLINVDFAD VKGIMSGAGT ALMGIGSARG DGRSLKAAEI AINSPLLEAS
260 270 280 290 300
MEGAQGVLMS IAGGSDLGLF EINEAASLVQ DAAHPDANII FGTVIDDSLG
310 320 330 340 350
DEVRVTVIAA GFEANGPGRT PVMGSTGGAH RIESAKAGAL TSTLFEPVDA
360 370
ASAPLHTNGA ALSIGGDDDD VDVPPFMRR
Length:379
Mass (Da):38,605
Last modified:June 1, 2001 - v1
Checksum:i3837589C30164F79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583920 Genomic DNA. Translation: CAC31298.1.
PIRiG87023.
RefSeqiNP_301700.1. NC_002677.1.
WP_010908024.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31298; CAC31298; CAC31298.
GeneIDi909912.
KEGGimle:ML0917.
PATRICi18053430. VBIMycLep78757_1660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583920 Genomic DNA. Translation: CAC31298.1.
PIRiG87023.
RefSeqiNP_301700.1. NC_002677.1.
WP_010908024.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ9CCE4.
SMRiQ9CCE4. Positions 22-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0917.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31298; CAC31298; CAC31298.
GeneIDi909912.
KEGGimle:ML0917.
PATRICi18053430. VBIMycLep78757_1660.

Organism-specific databases

LepromaiML0917.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiAQVIWGI.
OrthoDBiPOG091H02KK.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ. 1 hit.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFTSZ_MYCLE
AccessioniPrimary (citable) accession number: Q9CCE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.