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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Binding sitei136GTPUniRule annotation2 Publications1
Binding sitei140GTPUniRule annotation2 Publications1
Binding sitei184GTPUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 22GTPUniRule annotation2 Publications5
Nucleotide bindingi105 – 107GTPUniRule annotation2 Publications3

GO - Molecular functioni

  • GTPase activity Source: MTBBASE
  • GTP binding Source: UniProtKB-HAMAP
  • magnesium ion binding Source: MTBBASE

GO - Biological processi

  • barrier septum assembly Source: MTBBASE
  • cell cycle Source: MTBBASE
  • FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
  • growth Source: MTBBASE
  • protein polymerization Source: MTBBASE
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6358-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:Rv2150c
ORF Names:MTCY270.18
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2150c.

Subcellular locationi

  • Cytoplasm UniRule annotation

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

GO - Cellular componenti

  • cell division site Source: UniProtKB-HAMAP
  • cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

ChEMBLiCHEMBL4213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001143651 – 379Cell division protein FtsZAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei343Phosphothreonine1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP9WN95.

PTM databases

iPTMnetiP9WN95.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
crgAP9WP575EBI-6414519,EBI-6414478

Protein-protein interaction databases

IntActiP9WN95. 1 interactor.
STRINGi83332.Rv2150c.

Chemistry databases

BindingDBiP9WN95.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 16Combined sources6
Helixi17 – 29Combined sources13
Beta strandi34 – 42Combined sources9
Helixi44 – 49Combined sources6
Beta strandi53 – 57Combined sources5
Turni60 – 62Combined sources3
Helixi72 – 81Combined sources10
Helixi83 – 90Combined sources8
Beta strandi94 – 101Combined sources8
Helixi106 – 121Combined sources16
Beta strandi124 – 131Combined sources8
Helixi134 – 136Combined sources3
Helixi138 – 154Combined sources17
Beta strandi156 – 162Combined sources7
Helixi163 – 166Combined sources4
Helixi176 – 199Combined sources24
Helixi208 – 215Combined sources8
Beta strandi219 – 230Combined sources12
Helixi233 – 242Combined sources10
Helixi245 – 247Combined sources3
Helixi251 – 253Combined sources3
Beta strandi255 – 263Combined sources9
Helixi269 – 282Combined sources14
Beta strandi288 – 295Combined sources8
Helixi297 – 299Combined sources3
Beta strandi302 – 310Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP9WN95.
SMRiP9WN95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
KOiK03531.
OMAiAQVIWGI.
PhylomeDBiP9WN95.

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.
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.

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
Checksum:i3F580353078788A9
GO

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_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44926; CCP44926; Rv2150c.
GeneIDi888369.
KEGGimtu:Rv2150c.

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_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP9WN95.
SMRiP9WN95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WN95. 1 interactor.
STRINGi83332.Rv2150c.

Chemistry databases

BindingDBiP9WN95.
ChEMBLiCHEMBL4213.

PTM databases

iPTMnetiP9WN95.

Proteomic databases

PaxDbiP9WN95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44926; CCP44926; Rv2150c.
GeneIDi888369.
KEGGimtu:Rv2150c.

Organism-specific databases

TubercuListiRv2150c.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
KOiK03531.
OMAiAQVIWGI.
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.
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_MYCTU
AccessioniPrimary (citable) accession number: P9WN95
Secondary accession number(s): L0TBN4, O08378, P64170
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 22 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.