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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Unreviewed-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 sitei161 – 1611GTPUniRule annotation
Binding sitei164 – 1641GTPUniRule annotation
Binding sitei207 – 2071GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 475GTPUniRule annotation
Nucleotide bindingi130 – 1323GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, SeptationUniRule annotation

Keywords - Ligandi

GTP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciMACE188937:GI2O-3921-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:MA_3876Imported
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)Imported
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000002487 Componenti: Chromosome

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

CytoplasmUniRule annotation

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

STRINGi188937.MA3876.

Structurei

3D structure databases

ProteinModelPortaliQ8TJB2.
SMRiQ8TJB2. Positions 32-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 225191TubulinInterPro annotationAdd
BLAST
Domaini227 – 344118Tubulin_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG02201. Archaea.
COG0206. LUCA.
InParanoidiQ8TJB2.
KOiK03531.
OMAiIMNQGGV.
PhylomeDBiQ8TJB2.

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8TJB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSIVQEAMK FSEKEKEYRK NSSSEEDIEE FGQPRIMIVG CGGAGNNTVN
60 70 80 90 100
RLYNIGIEGA ETVCINTDKQ HLDNVRADKK ILVGKTLTRG LGAGGYPETG
110 120 130 140 150
KKAAELARGT LEEVLKNVDL VFITAGLGGG TGTGVAPVVA EVAKEQGAIV
160 170 180 190 200
VGMVSSPFRV ERARIFKAEE GLEDLRRAAD TVIVLDNNRL LNYVPNLPID
210 220 230 240 250
QAFSVMDQLI AETVKGITET ITVPSLINLD YADIRTIMSC GGVAVMLVGE
260 270 280 290 300
SKSQDKSTEV VRTALNHPLL DVDYKGATGS LVHVTGGPDL SLKEAEEIAS
310 320 330 340 350
MLTYELSSSA NVIWGARIRE DYEGRVRVMA IMTGVQSAQI LGPQAGAGIF
360 370 380 390
ESRAEAEPIQ EKRFGRLSPG RRGETAGPLR KKHEESIIDF IN
Length:392
Mass (Da):42,262
Last modified:June 1, 2002 - v1
Checksum:i814A805D3097D832
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM07227.1.
RefSeqiWP_011023772.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM07227; AAM07227; MA_3876.
GeneIDi1475769.
KEGGimac:MA_3876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM07227.1.
RefSeqiWP_011023772.1. NC_003552.1.

3D structure databases

ProteinModelPortaliQ8TJB2.
SMRiQ8TJB2. Positions 32-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi188937.MA3876.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM07227; AAM07227; MA_3876.
GeneIDi1475769.
KEGGimac:MA_3876.

Phylogenomic databases

eggNOGiarCOG02201. Archaea.
COG0206. LUCA.
InParanoidiQ8TJB2.
KOiK03531.
OMAiIMNQGGV.
PhylomeDBiQ8TJB2.

Enzyme and pathway databases

BioCyciMACE188937:GI2O-3921-MONOMER.

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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ8TJB2_METAC
AccessioniPrimary (citable) accession number: Q8TJB2
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: September 7, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.