P17865 (FTSZ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division protein FtsZ

Gene names

Name:	ftsZ
Ordered Locus Names:	BSU15290

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6
Subunit structure	Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner By similarity. Interacts directly with several other division proteins By similarity. Interacts with FtsA. Ref.6
Subcellular location	Cytoplasm By similarity. Note: Assembles at midcell at the inner surface of the cytoplasmic membrane By similarity.
Sequence similarities	Belongs to the FtsZ family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Septation
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	barrier septum assembly Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis by binary fission Inferred from electronic annotation. Source: HAMAP protein polymerization Inferred from electronic annotation. Source: HAMAP
Cellular_component	cell division site part Inferred from electronic annotation. Source: HAMAP cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-1569853,EBI-1569853
ezrA	O34894	4	EBI-1569853,EBI-1567579
ftsA	P28264	7	EBI-1569853,EBI-2122615
sepF	O31728	6	EBI-1569853,EBI-2122748
ugtP	P54166	3	EBI-1569853,EBI-1567571
zapA	P94542	4	EBI-1569853,EBI-2122911

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

Cell division protein FtsZ HAMAP-Rule MF_00909

PRO_0000114341

Regions

Nucleotide binding

104 – 112

9

GTP Potential

Experimental info

Sequence conflict

345 – 346

2

EP → DA in AAA22457. Ref.1

Secondary structure

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382

Helix Strand Turn

Details...

Beta strand

14 – 19

6

Helix

20 – 32

13

Beta strand

39 – 46

8

Helix

47 – 51

5

Beta strand

56 – 60

5

Helix

63 – 66

4

Helix

75 – 84

10

Helix

86 – 93

8

Beta strand

97 – 108

12

Helix

109 – 123

15

Beta strand

127 – 134

8

Helix

137 – 139

3

Helix

141 – 157

17

Beta strand

159 – 165

7

Helix

166 – 172

7

Helix

179 – 198

20

Turn

199 – 201

3

Beta strand

205 – 207

3

Helix

211 – 217

7

Beta strand

221 – 233

13

Helix

236 – 245

10

Helix

254 – 256

3

Beta strand

258 – 266

9

Helix

272 – 285

14

Beta strand

291 – 298

8

Beta strand

303 – 315

13

Sequences

	Sequence		Length	Mass (Da)
	P17865 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 24E908DEC9685614	FASTA	382	40,395
	10 20 30 40 50 60 MLEFETNIDG LASIKVIGVG GGGNNAVNRM IENEVQGVEY IAVNTDAQAL NLSKAEVKMQ 70 80 90 100 110 120 IGAKLTRGLG AGANPEVGKK AAEESKEQIE EALKGADMVF VTAGMGGGTG TGAAPVIAQI 130 140 150 160 170 180 AKDLGALTVG VVTRPFTFEG RKRQLQAAGG ISAMKEAVDT LIVIPNDRIL EIVDKNTPML 190 200 210 220 230 240 EAFREADNVL RQGVQGISDL IATPGLINLD FADVKTIMSN KGSALMGIGI ATGENRAAEA 250 260 270 280 290 300 AKKAISSPLL EAAIDGAQGV LMNITGGTNL SLYEVQEAAD IVASASDQDV NMIFGSVINE 310 320 330 340 350 360 NLKDEIVVTV IATGFIEQEK DVTKPQRPSL NQSIKTHNQS VPKREPKREE PQQQNTVSRH 370 380 TSQPADDTLD IPTFLRNRNK RG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA." Beall B., Lowe M., Lutkenhaus J. J. Bacteriol. 170:4855-4864(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 345-346.
[4]	"Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis." Wu X.-C., Nathoo S., Pang A.S.-H., Carne T., Wang S.-L. J. Biol. Chem. 265:6845-6850(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-382.
[5]	"Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins." Anderson D.E., Gueiros-Filho F.J., Erickson H.P. J. Bacteriol. 186:5775-5781(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: JDB401.
[6]	"Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly." Jensen S.O., Thompson L.S., Harry E.J. J. Bacteriol. 187:6536-6544(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FTSA. Strain: 168.
[7]	"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 (2.5 ANGSTROMS).
[8]	"An inhibitor of FtsZ with potent and selective anti-staphylococcal activity." Haydon D.J., Stokes N.R., Ure R., Galbraith G., Bennett J.M., Brown D.R., Baker P.J., Barynin V.V., Rice D.W., Sedelnikova S.E., Heal J.R., Sheridan J.M., Aiwale S.T., Chauhan P.K., Srivastava A., Taneja A., Collins I., Errington J., Czaplewski L.G. Science 321:1673-1675(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[9]	"Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer." Raymond A., Lovell S., Lorimer D., Walchli J., Mixon M., Wallace E., Thompkins K., Archer K., Burgin A., Stewart L. BMC Biotechnol. 9:37-37(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 12-315.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22630 Genomic DNA. Translation: AAA22457.1.
AL009126 Genomic DNA. Translation: CAB13402.2.
J05400 Genomic DNA. Translation: AAA83361.1.

PIR

I39848.

RefSeq

NP_389412.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RHH	X-ray	2.00	A	12-315	[»]
2RHJ	X-ray	1.76	A	12-315	[»]
2RHL	X-ray	2.45	A/B	12-315	[»]
2RHO	X-ray	2.45	A/B	12-315	[»]
2VAM	X-ray	2.50	A	1-382	[»]
2VXY	X-ray	1.70	A	1-382	[»]

ProteinModelPortal

P17865.

SMR

P17865. Positions 11-316.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17865. 8 interactions.

STRING

224308.BSU15290.

Proteomic databases

PaxDb

P17865.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13402; CAB13402; BSU15290.

GeneID

935971.

KEGG

bsu:BSU15290.

PATRIC

18974863. VBIBacSub10457_1623.

Organism-specific databases

GenoList

BSU15290. [Micado]

Phylogenomic databases

eggNOG

COG0206.

HOGENOM

HOG000049094.

KO

K03531.

ProtClustDB

PRK09330.

Enzyme and pathway databases

BioCyc

BSUB:BSU15290-MONOMER.

Family and domain databases

Gene3D

3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.

HAMAP

MF_00909. FtsZ.

InterPro

IPR000158. 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]

Pfam

PF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]

PRINTS

PR00423. CELLDVISFTSZ.

SMART

SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]

SUPFAM

SSF55307. Tub_FtsZ_C. 1 hit.
SSF52490. Tubulin_FtsZ. 1 hit.

TIGRFAMs

TIGR00065. ftsZ. 1 hit.

PROSITE

PS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P17865.

ChEMBL

CHEMBL5690.

EvolutionaryTrace

P17865.

Entry information

Entry name

FTSZ_BACSU

Accession

Primary (citable) accession number: P17865

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program