Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361GTPUniRule annotation2 Publications
Binding sitei140 – 1401GTPUniRule annotation2 Publications
Binding sitei184 – 1841GTPUniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225GTPUniRule annotation2 Publications
Nucleotide bindingi105 – 1073GTPUniRule annotation2 Publications

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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi135 – 1351F → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi137 – 1371G → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi138 – 1381K → A: Decrease in GTPase activity. 1 Publication
Mutagenesisi164 – 1641D → A: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi176 – 1761L → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi179 – 1791A → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi203 – 2031L → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi204 – 2041I → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi210 – 2101D → G: Reduces FtsZ polymerization and GTP hydrolysis. Does not affect the structure or the stability of the unpolymerized FtsZ. 1 Publication
Mutagenesisi269 – 2691L → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi289 – 2891I → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi291 – 2911F → E: Strong decrease in GTPase activity. 1 Publication
Mutagenesisi343 – 3431T → A: Lack of phosphorylation. 1 Publication

Chemistry

ChEMBLiCHEMBL4213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Cell division protein FtsZPRO_0000114365Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei343 – 3431Phosphothreonine1 Publication

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 interaction.
STRINGi83332.Rv2150c.

Chemistry

BindingDBiP9WN95.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 166Combined sources
Helixi17 – 2913Combined sources
Beta strandi34 – 429Combined sources
Helixi44 – 496Combined sources
Beta strandi53 – 575Combined sources
Turni60 – 623Combined sources
Helixi72 – 8110Combined sources
Helixi83 – 908Combined sources
Beta strandi94 – 1018Combined sources
Helixi106 – 12116Combined sources
Beta strandi124 – 1318Combined sources
Helixi134 – 1363Combined sources
Helixi138 – 15417Combined sources
Beta strandi156 – 1627Combined sources
Helixi163 – 1664Combined sources
Helixi176 – 19924Combined sources
Helixi208 – 2158Combined sources
Beta strandi219 – 23012Combined sources
Helixi233 – 24210Combined sources
Helixi245 – 2473Combined sources
Helixi251 – 2533Combined sources
Beta strandi255 – 2639Combined sources
Helixi269 – 28214Combined sources
Beta strandi288 – 2958Combined sources
Helixi297 – 2993Combined sources
Beta strandi302 – 3109Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 22-312.
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

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
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
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. Positions 22-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WN95. 1 interaction.
STRINGi83332.Rv2150c.

Chemistry

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.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division."
    Sureka K., Hossain T., Mukherjee P., Chatterjee P., Datta P., Kundu M., Basu J.
    PLoS ONE 5:E8590-E8590(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHAB AND FTSQ, PHOSPHORYLATION AT THR-343, MUTAGENESIS OF THR-343.
    Strain: ATCC 25618 / H37Rv.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  4. "Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches."
    Leung A.K., Lucile White E., Ross L.J., Reynolds R.C., DeVito J.A., Borhani D.W.
    J. Mol. Biol. 342:953-970(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH GDP, SUBUNIT.
  5. "Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery."
    Respicio L., Nair P.A., Huang Q., Anil B., Tracz S., Truglio J.J., Kisker C., Raleigh D.P., Ojima I., Knudson D.L., Tonge P.J., Slayden R.A.
    Tuberculosis 88:420-429(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, GTPASE ACTIVITY, MUTAGENESIS OF ASP-210.
    Strain: ATCC 25618 / H37Rv.
  6. "FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation."
    Li Y., Hsin J., Zhao L., Cheng Y., Shang W., Huang K.C., Wang H.W., Ye S.
    Science 341:392-395(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) IN COMPLEX WITH GDP, SUBUNIT, MUTAGENESIS OF PHE-135; GLY-137; LYS-138; ASP-164; LEU-176; ALA-179; LEU-203; ILE-204; LEU-269; ILE-289 AND PHE-291.

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: January 20, 2016
This is version 20 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.