Cell division protein FtsZ

Details

Name
Cell division protein FtsZ
Synonyms
Not Available
Gene Name
ftsZ
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Amino acid sequence
>lcl|BSEQ0011297|Cell division protein FtsZ
MGFDLDVEKKKENRNIPQANNLKIKVIGVGGAGNNAINRMIEIGIHGVEFVAVNTDLQVL
EASNADVKIQIGENITRGLGAGGRPEIGEQAALESEEKIREVLQDTHMVFITAGFGGGTG
TGASPVIAKIAKEMGILTVAIVTTPFYFEGPERLKKAIEGLKKLRKHVDTLIKISNNKLM
EELPRDVKIKDAFLKADETLHQGVKGISELITKRGYINLDFADIESVMKDAGAAILGIGV
GKGEHRAREAAKKAMESKLIEHPVENASSIVFNITAPSNIRMEEVHEAAMIIRQNSSEDA
DVKFGLIFDDEVPDDEIRVIFIATRFPDEDKILFPEGDIPAIYRYGLEGLL
Number of residues
351
Molecular Weight
38306.67
Theoretical pI
5.02
GO Classification
Functions
GTP binding / GTPase activity
Processes
barrier septum assembly / FtsZ-dependent cytokinesis / protein polymerization
Components
cell division site / cytoplasm
General Function
Gtpase activity
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011298|Cell division protein FtsZ (ftsZ)
ATGGGATTTGACCTTGATGTTGAGAAGAAAAAGGAAAATAGAAACATCCCTCAGGCGAAC
AATTTGAAGATAAAAGTCATAGGTGTAGGCGGTGCCGGAAACAATGCCATAAACAGAATG
ATAGAAATAGGAATACACGGTGTTGAATTTGTCGCGGTGAACACCGATCTTCAGGTACTG
GAGGCTTCTAACGCTGACGTGAAGATTCAGATCGGTGAGAACATCACACGAGGCCTTGGT
GCAGGGGGACGTCCCGAGATAGGAGAACAAGCTGCTCTTGAGAGCGAGGAAAAAATCAGA
GAAGTGCTCCAGGATACCCACATGGTCTTCATAACTGCAGGGTTCGGAGGAGGGACGGGA
ACAGGTGCTTCCCCTGTCATAGCAAAGATAGCCAAAGAAATGGGAATCCTGACTGTAGCC
ATAGTGACGACTCCCTTCTATTTCGAAGGCCCGGAGAGACTCAAAAAAGCGATAGAGGGG
CTCAAAAAACTTCGAAAACATGTGGATACCCTCATAAAGATATCCAACAACAAACTCATG
GAAGAACTCCCGAGGGATGTCAAGATAAAGGATGCTTTTCTGAAGGCTGACGAGACTCTT
CACCAGGGAGTGAAAGGAATTTCGGAACTGATAACGAAGAGGGGTTACATAAATCTCGAC
TTTGCAGACATAGAGTCGGTAATGAAGGACGCCGGTGCTGCGATCCTTGGCATAGGTGTT
GGAAAGGGAGAACACAGAGCGAGAGAAGCTGCTAAGAAGGCTATGGAAAGCAAGTTGATA
GAGCATCCTGTAGAAAATGCGAGTTCGATTGTGTTCAATATAACTGCTCCCAGCAATATA
AGAATGGAGGAAGTGCACGAAGCAGCTATGATCATAAGGCAGAACAGCAGTGAGGACGCG
GACGTCAAATTCGGTCTCATCTTCGATGATGAAGTACCCGATGACGAAATACGTGTGATC
TTCATAGCTACAAGATTCCCAGATGAAGACAAGATTCTATTCCCGGAAGGTGACATACCG
GCCATTTACAGATACGGTCTGGAGGGGCTTCTTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO08398
UniProtKB Entry NameFTSZ_THEMA
GenBank Protein ID2104497
GenBank Gene IDU65944
General References
  1. Lu C, Stricker J, Erickson HP: FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly. Cell Motil Cytoskeleton. 1998;40(1):71-86. [Article]
  2. Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [Article]
  3. Oliva MA, Cordell SC, Lowe J: Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. Epub 2004 Nov 21. [Article]
  4. Szwedziak P, Wang Q, Freund SM, Lowe J: FtsA forms actin-like protofilaments. EMBO J. 2012 May 16;31(10):2249-60. doi: 10.1038/emboj.2012.76. Epub 2012 Mar 30. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03532Phosphomethylphosphonic acid guanylate esterexperimentalunknownDetails