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Protein

Cell division protein FtsZ 1

Gene

ftsZ1

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei165 – 1651GTPUniRule annotation3 Publications
Binding sitei169 – 1691GTPUniRule annotation2 Publications
Binding sitei212 – 2121GTPUniRule annotation3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi47 – 482GTP3 Publications
Nucleotide bindingi97 – 993GTP1 Publication
Nucleotide bindingi134 – 1363GTPUniRule annotation3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.5.6. 3260.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZ 1UniRule annotation
Gene namesi
Name:ftsZ1UniRule annotation
Ordered Locus Names:MJ0370
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 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

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Cell division protein FtsZ 1PRO_0000114401Add
BLAST

Interactioni

Subunit structurei

Homodimer (PubMed:15558053). Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins (By similarity).UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_0370.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Helixi24 – 3411Combined sources
Beta strandi40 – 456Combined sources
Helixi46 – 5914Combined sources
Beta strandi64 – 729Combined sources
Helixi73 – 775Combined sources
Beta strandi82 – 865Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 953Combined sources
Helixi101 – 11010Combined sources
Helixi112 – 1198Combined sources
Beta strandi123 – 1308Combined sources
Helixi135 – 14915Combined sources
Beta strandi153 – 1608Combined sources
Helixi163 – 1653Combined sources
Helixi167 – 18115Combined sources
Beta strandi185 – 1917Combined sources
Helixi192 – 1943Combined sources
Helixi195 – 1984Combined sources
Beta strandi199 – 2013Combined sources
Helixi204 – 22724Combined sources
Helixi236 – 2438Combined sources
Beta strandi247 – 25610Combined sources
Beta strandi258 – 2603Combined sources
Helixi261 – 27010Combined sources
Helixi279 – 2813Combined sources
Beta strandi284 – 2918Combined sources
Helixi297 – 31014Combined sources
Beta strandi316 – 3238Combined sources
Turni326 – 3294Combined sources
Beta strandi331 – 3388Combined sources
Helixi341 – 3433Combined sources
Beta strandi344 – 3474Combined sources
Beta strandi350 – 3534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSZX-ray2.80A1-364[»]
1W58X-ray2.5011-364[»]
1W59X-ray2.70A/B1-364[»]
1W5AX-ray2.40A/B1-364[»]
1W5BX-ray2.20A/B1-364[»]
1W5EX-ray3.00A/B/C/D/E/F/G/H/I1-364[»]
2VAPX-ray1.70A1-364[»]
ProteinModelPortaliQ57816.
SMRiQ57816. Positions 22-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57816.

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG02201. Archaea.
COG0206. LUCA.
InParanoidiQ57816.
KOiK03531.
OMAiGMAMMGI.
PhylomeDBiQ57816.

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.

Q57816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLKNVLEE GSKLEEFNEL ELSPEDKELL EYLQQTKAKI TVVGCGGAGN
60 70 80 90 100
NTITRLKMEG IEGAKTVAIN TDAQQLIRTK ADKKILIGKK LTRGLGAGGN
110 120 130 140 150
PKIGEEAAKE SAEEIKAAIQ DSDMVFITCG LGGGTGTGSA PVVAEISKKI
160 170 180 190 200
GALTVAVVTL PFVMEGKVRM KNAMEGLERL KQHTDTLVVI PNEKLFEIVP
210 220 230 240 250
NMPLKLAFKV ADEVLINAVK GLVELITKDG LINVDFADVK AVMNNGGLAM
260 270 280 290 300
IGIGESDSEK RAKEAVSMAL NSPLLDVDID GATGALIHVM GPEDLTLEEA
310 320 330 340 350
REVVATVSSR LDPNATIIWG ATIDENLENT VRVLLVITGV QSRIEFTDTG
360
LKRKKLELTG IPKI
Length:364
Mass (Da):38,924
Last modified:November 1, 1996 - v1
Checksum:i3BB386A5D2FCA107
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98359.1.
PIRiB64346.

Genome annotation databases

EnsemblBacteriaiAAB98359; AAB98359; MJ_0370.
KEGGimja:MJ_0370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98359.1.
PIRiB64346.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSZX-ray2.80A1-364[»]
1W58X-ray2.5011-364[»]
1W59X-ray2.70A/B1-364[»]
1W5AX-ray2.40A/B1-364[»]
1W5BX-ray2.20A/B1-364[»]
1W5EX-ray3.00A/B/C/D/E/F/G/H/I1-364[»]
2VAPX-ray1.70A1-364[»]
ProteinModelPortaliQ57816.
SMRiQ57816. Positions 22-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98359; AAB98359; MJ_0370.
KEGGimja:MJ_0370.

Phylogenomic databases

eggNOGiarCOG02201. Archaea.
COG0206. LUCA.
InParanoidiQ57816.
KOiK03531.
OMAiGMAMMGI.
PhylomeDBiQ57816.

Enzyme and pathway databases

BRENDAi3.6.5.6. 3260.

Miscellaneous databases

EvolutionaryTraceiQ57816.

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 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Crystal structure of the bacterial cell-division protein ftsZ."
    Loewe J., Amos L.A.
    Nature 391:203-206(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP.
  3. "Crystal structure determination of FtsZ from Methanococcus jannaschii."
    Loewe J.
    J. Struct. Biol. 124:235-243(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-356.
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  4. "Structural insights into FtsZ protofilament formation."
    Oliva M.A., Cordell S.C., Lowe J.
    Nat. Struct. Mol. Biol. 11:1243-1250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GTP, SUBUNIT.
  5. "Structural insights into the conformational variability of FtsZ."
    Oliva M.A., Trambaiolo D., Lowe J.
    J. Mol. Biol. 373:1229-1242(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GDP.

Entry informationi

Entry nameiFTSZ1_METJA
AccessioniPrimary (citable) accession number: Q57816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 20, 2016
This is version 113 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. Methanococcus jannaschii
    Methanococcus jannaschii: 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.