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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei148GTPUniRule annotation1
Binding sitei152GTPUniRule annotation1
Binding sitei196GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi30 – 34GTPUniRule annotation5
Nucleotide bindingi117 – 119GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division, Septation
LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:BB_0299
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliella
Proteomesi
  • UP000001807 Componenti: Chromosome

Subcellular locationi

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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001143431 – 399Cell division protein FtsZAdd BLAST399

Proteomic databases

PRIDEiP45483.

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

STRINGi224326.BB_0299.

Structurei

3D structure databases

ProteinModelPortaliP45483.
SMRiP45483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
KOiK03531.
OMAiMRAVKGI.

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.
InterProiView protein in InterPro
IPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR037103. Tubulin/FtsZ_C_sf.
IPR036525. Tubulin/FtsZ_GTPase_sf.
IPR003008. Tubulin_FtsZ_GTPase.
PfamiView protein in Pfam
PF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiView protein in SMART
SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiView protein in PROSITE
PS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P45483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDYNMIDSH TRRFDSTTNP TILKVIGAGG GGSNAVNRMI EYGVRDVEFI
60 70 80 90 100
VANTDLQALQ TSIAPIKIAL GAKVTAGLGA GGKPEIGQAA AEEDIDVIRN
110 120 130 140 150
HLSGADMVFI TAGMGGGTGT GAAPVIAQVA KELGILTVGV VTKPFKFEGP
160 170 180 190 200
KKLRLAEQGI NNLRKSVDTL IIIPNQKLLT VVDKRTTIKD AFKRADDVLR
210 220 230 240 250
MGVQGIAGLI IEHGEVNIDF ADVKSIMQGQ GDALMGIGYG KGENRAVDAA
260 270 280 290 300
TSAISNPLLE EVRIEGSKGL LVNVTGGDDF SLLELEEIMG IITVSVDDEA
310 320 330 340 350
TVIYGHAINS NLEDEIYVTV VATGFASKKQ KEISSTPENN TLSSKEFDTL
360 370 380 390
MSGNQNAPSG SYEQQDSSFA AKSKNVNYFD DDIDVPTFLR NLNKKSSDD
Length:399
Mass (Da):42,398
Last modified:December 15, 1998 - v3
Checksum:iE808E336343EE583
GO

Sequence cautioni

The sequence AAA85622 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA65464 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA78156 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115G → A (PubMed:1490605).Curated1
Sequence conflicti115G → A (Ref. 5) Curated1
Sequence conflicti249 – 250AA → RR in CAA65464 (Ref. 3) Curated2
Sequence conflicti249 – 250AA → RR in AAB51402 (Ref. 3) Curated2
Sequence conflicti336T → A in CAA65464 (Ref. 3) Curated1
Sequence conflicti336T → A in AAB51402 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43739 Genomic DNA. Translation: AAA85622.1. Different initiation.
AE000783 Genomic DNA. Translation: AAC66649.2.
X96685 Genomic DNA. Translation: CAA65464.1. Different initiation.
L76303 Genomic DNA. Translation: AAB51402.1.
Z12164 Genomic DNA. Translation: CAA78156.1. Different initiation.
PIRiC70137.
RefSeqiNP_212433.2. NC_001318.1.
WP_002656388.1. NC_001318.1.

Genome annotation databases

EnsemblBacteriaiAAC66649; AAC66649; BB_0299.
GeneIDi1195136.
KEGGibbu:BB_0299.
PATRICifig|224326.49.peg.698.

Similar proteinsi

Entry informationi

Entry nameiFTSZ_BORBU
AccessioniPrimary (citable) accession number: P45483
Secondary accession number(s): Q59183
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: October 25, 2017
This is version 118 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome