P64170 (FTSZ_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division protein FtsZ

Gene names

Name:	ftsZ
Ordered Locus Names:	Rv2150c, MT2209
ORF Names:	MTCY270.18

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	379 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 By similarity. Binds GTP and shows GTPase activity. HAMAP MF_00909
Subunit structure	Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins By similarity. Ref.3
Subcellular location	Cytoplasm By similarity. Note: Assembles at midcell at the inner surface of the cytoplasmic membrane By similarity. HAMAP MF_00909
Sequence similarities	Belongs to the FtsZ family.
Sequence caution	The sequence AAK46493.1 differs from that shown. Reason: Erroneous initiation.

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 mutant phenotype. Source: MTBBASE cell cycle Inferred from mutant phenotype. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE protein polymerization Inferred from direct assay. Source: MTBBASE
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE protein complex Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay. Source: MTBBASE magnesium ion binding Inferred from direct assay. Source: MTBBASE protein binding Inferred from physical interaction. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Cell division protein FtsZ HAMAP MF_00909

PRO_0000114365

Regions

Nucleotide binding

101 – 109

9

GTP Potential

Experimental info

Mutagenesis

210

1

D → G: Reduces FtsZ polymerization and GTP hydrolysis. Does not affect the structure or the stability of the unpolymerized FtsZ. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

379

Helix Strand Turn

Details...

Beta strand

11 – 16

6

Helix

17 – 29

13

Beta strand

36 – 42

7

Helix

44 – 48

5

Beta strand

53 – 58

6

Helix

60 – 63

4

Helix

72 – 81

10

Helix

83 – 90

8

Beta strand

94 – 101

8

Helix

106 – 120

15

Beta strand

124 – 131

8

Helix

134 – 136

3

Helix

138 – 154

17

Beta strand

156 – 162

7

Helix

163 – 166

4

Helix

176 – 199

24

Helix

208 – 215

8

Beta strand

219 – 230

12

Helix

233 – 243

11

Helix

245 – 247

3

Helix

251 – 253

3

Beta strand

255 – 263

9

Helix

269 – 282

14

Beta strand

288 – 295

8

Helix

297 – 299

3

Beta strand

302 – 310

9

Sequences

	Sequence		Length	Mass (Da)
	P64170 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 3F580353078788A9	FASTA	379	38,756
	10 20 30 40 50 60 MTPPHNYLAV IKVVGIGGGG VNAVNRMIEQ GLKGVEFIAI NTDAQALLMS DADVKLDVGR 70 80 90 100 110 120 DSTRGLGAGA DPEVGRKAAE DAKDEIEELL RGADMVFVTA GEGGGTGTGG APVVASIARK 130 140 150 160 170 180 LGALTVGVVT RPFSFEGKRR SNQAENGIAA LRESCDTLIV IPNDRLLQMG DAAVSLMDAF 190 200 210 220 230 240 RSADEVLLNG VQGITDLITT PGLINVDFAD VKGIMSGAGT ALMGIGSARG EGRSLKAAEI 250 260 270 280 290 300 AINSPLLEAS MEGAQGVLMS IAGGSDLGLF EINEAASLVQ DAAHPDANII FGTVIDDSLG 310 320 330 340 350 360 DEVRVTVIAA GFDVSGPGRK PVMGETGGAH RIESAKAGKL TSTLFEPVDA VSVPLHTNGA 370 TLSIGGDDDD VDVPPFMRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches." Leung A.K., Lucile White E., Ross L.J., Reynolds R.C., DeVito J.A., Borhani D.W. J. Mol. Biol. 342:953-970(2004) [PubMed: 15342249] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), SUBUNIT.
[4]	"Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery." Respicio L., Nair P.A., Huang Q., Anil B., Tracz S., Truglio J.J., Kisker C., Raleigh D.P., Ojima I., Knudson D.L., Tonge P.J., Slayden R.A. Tuberculosis 88:420-429(2008) [PubMed: 18479968] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, GTPASE ACTIVITY, MUTAGENESIS OF ASP-210. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842578 Genomic DNA. Translation: CAB08643.1.
AE000516 Genomic DNA. Translation: AAK46493.1. Different initiation.

PIR

B70579.

RefSeq

NP_216666.1. NC_000962.2.
NP_336679.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RLU	X-ray	2.08	A/B	1-379	[»]
1RQ2	X-ray	1.86	A/B	1-379	[»]
1RQ7	X-ray	2.60	A/B	1-379	[»]
2Q1X	X-ray	2.35	A/B	1-379	[»]
2Q1Y	X-ray	2.30	A/B	1-379	[»]

ProteinModelPortal

P64170.

SMR

P64170. Positions 22-312.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-13159N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001413; EBMYCP00000001413; EBMYCG00000001413.
EBMYCT00000072368; EBMYCP00000070427; EBMYCG00000072363.

GeneID

888369.
924252.

GenomeReviews

Gene locus MT2209 in contig AE000516_GR.
Gene locus Rv2150c in contig AL123456_GR.

KEGG

mtc:MT2209.
mtu:Rv2150c.

PATRIC

18126616. VBIMycTub22151_2420.

TIGR

MT2209.

Organism-specific databases

TubercuList

Rv2150c.

Phylogenomic databases

GeneTree

EBGT00050000017272.

HOGENOM

HBG478075.

OMA

VLRMGVK.

PhylomeDB

P64170.

ProtClustDB

PRK09330.

Family and domain databases

HAMAP

MF_00909. FtsZ.
[Tree]

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]

Gene3D

G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit.
G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.

KO

K03531.

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...

Entry information

Entry name

FTSZ_MYCTU

Accession

Primary (citable) accession number: P64170
Secondary accession number(s): O08378

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program