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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Borrelia recurrentis (strain A1)
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)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

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, SeptationUniRule annotation

Keywords - Ligandi

GTP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotationImported
Ordered Locus Names:BRE_306Imported
OrganismiBorrelia recurrentis (strain A1)Imported
Taxonomic identifieri412418 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorrelia
Proteomesi
  • UP000000612 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 214TubulinInterPro annotationAdd BLAST193
Domaini216 – 334Tubulin_CInterPro annotationAdd BLAST119

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000049094.
KOiK03531.
OMAiGMAMMGI.
OrthoDBiPOG091H02KK.

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.

B5RRB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDYNIIDSH SKRFDSATNP TVLKVIGAGG GGSNAVNRMI EYGVRDVEFI
60 70 80 90 100
VANTDLQALQ TSIAPIKIAL GAKVTAGLGA GGRPEIGQAA AEEDIDVIKN
110 120 130 140 150
HLAGADMVFI TAGMGGGTGT GAAPVIAQVA KELGILTVGV VTKPFKFEGP
160 170 180 190 200
KKMRLAEQGI NNLRKSVDTL IIIPNQKLLT VVDKRTTIKD AFKRADDVLR
210 220 230 240 250
MGVQGIAGLI IEHGEVNIDF ADVKSIMQGQ GDALMGIGYG KGENRAVDAA
260 270 280 290 300
TSAISNPLLE EVRIEGSKGL LVNITGGEDF SLLELEEIMG IITASVDDEA
310 320 330 340 350
TVIYGHAINS NLDDEIYVTV VATGFSAKKQ KDLSGVVENN TLSSKEFDSL
360 370 380 390
MSGSQDASGV TYGANDNFIA KSKNVNYFED DIDIPTFLRN LNKKNGDN
Length:398
Mass (Da):42,077
Last modified:November 4, 2008 - v1
Checksum:i41D7FD245F7D5147
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000993 Genomic DNA. Translation: ACH94552.1.
RefSeqiWP_012538804.1. NC_011244.1.

Genome annotation databases

EnsemblBacteriaiACH94552; ACH94552; BRE_306.
KEGGibre:BRE_306.
PATRICi20569763. VBIBorRec40566_0329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000993 Genomic DNA. Translation: ACH94552.1.
RefSeqiWP_012538804.1. NC_011244.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACH94552; ACH94552; BRE_306.
KEGGibre:BRE_306.
PATRICi20569763. VBIBorRec40566_0329.

Phylogenomic databases

HOGENOMiHOG000049094.
KOiK03531.
OMAiGMAMMGI.
OrthoDBiPOG091H02KK.

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 nameiB5RRB8_BORRA
AccessioniPrimary (citable) accession number: B5RRB8
Entry historyi
Integrated into UniProtKB/TrEMBL: November 4, 2008
Last sequence update: November 4, 2008
Last modified: November 30, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete 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.