Cell division protein FtsZ
Details
- Name
- Cell division protein FtsZ
- Synonyms
- Not Available
- Gene Name
- ftsZ
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051239|Cell division protein FtsZ MTPPHNYLAVIKVVGIGGGGVNAVNRMIEQGLKGVEFIAINTDAQALLMSDADVKLDVGR DSTRGLGAGADPEVGRKAAEDAKDEIEELLRGADMVFVTAGEGGGTGTGGAPVVASIARK LGALTVGVVTRPFSFEGKRRSNQAENGIAALRESCDTLIVIPNDRLLQMGDAAVSLMDAF RSADEVLLNGVQGITDLITTPGLINVDFADVKGIMSGAGTALMGIGSARGEGRSLKAAEI AINSPLLEASMEGAQGVLMSIAGGSDLGLFEINEAASLVQDAAHPDANIIFGTVIDDSLG DEVRVTVIAAGFDVSGPGRKPVMGETGGAHRIESAKAGKLTSTLFEPVDAVSVPLHTNGA TLSIGGDDDDVDVPPFMRR
- Number of residues
- 379
- Molecular Weight
- 38755.52
- Theoretical pI
- Not Available
- GO Classification
- FunctionsGTP binding / GTPase activity / magnesium ion bindingProcessesbarrier septum assembly / cell cycle / growth / protein polymerizationComponentscell division site / cytoplasm / plasma membrane
- General 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.
- Specific Function
- Gtp binding
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0051240|Cell division protein FtsZ (ftsZ) ATGACCCCCCCGCACAACTACCTGGCCGTCATCAAGGTCGTGGGTATCGGTGGTGGCGGT GTCAACGCCGTCAACCGAATGATCGAGCAGGGCCTCAAAGGCGTGGAATTCATCGCGATC AACACCGACGCCCAGGCGTTGTTGATGAGCGATGCCGACGTCAAACTCGACGTCGGCCGC GACTCCACCCGCGGGCTGGGCGCCGGCGCCGATCCGGAGGTCGGCCGTAAGGCCGCCGAG GACGCCAAGGACGAGATCGAAGAGCTGCTGCGCGGTGCCGACATGGTGTTTGTCACCGCC GGCGAGGGGGGCGGAACCGGCACCGGGGGGGCACCCGTCGTCGCCAGCATCGCCCGCAAG CTGGGCGCGTTGACCGTCGGTGTGGTCACCCGGCCGTTCTCGTTCGAGGGCAAGCGACGC AGCAATCAGGCCGAAAATGGCATCGCGGCGCTGCGGGAGAGTTGCGACACCCTCATCGTG ATTCCCAACGACCGGTTGCTGCAGATGGGAGATGCCGCGGTATCGCTGATGGATGCTTTC CGTAGCGCCGACGAGGTGCTGCTCAACGGCGTGCAGGGCATCACCGACCTGATTACCACC CCGGGTCTAATCAACGTCGACTTCGCCGACGTCAAGGGCATCATGTCCGGTGCCGGCACC GCACTGATGGGCATCGGCTCGGCCCGGGGCGAAGGCCGGTCGCTCAAAGCGGCCGAGATC GCCATCAACTCGCCGTTGCTGGAAGCCTCGATGGAGGGCGCGCAAGGCGTGCTGATGTCG ATCGCCGGCGGCAGCGACTTGGGCTTGTTCGAGATCAACGAGGCGGCCTCGTTGGTACAA GACGCCGCTCACCCCGATGCCAACATCATCTTCGGCACCGTCATCGACGATTCGCTCGGT GACGAGGTGCGGGTGACCGTGATCGCGGCCGGCTTCGACGTCAGCGGTCCCGGCCGCAAG CCGGTGATGGGCGAGACCGGCGGCGCCCACCGGATCGAGTCAGCCAAGGCAGGCAAGCTC ACCTCGACCTTGTTCGAGCCGGTCGACGCCGTCAGCGTGCCGTTGCACACCAACGGCGCA ACCCTGAGCATCGGCGGTGATGACGACGATGTCGACGTGCCGCCCTTCATGCGCCGCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WN95 UniProtKB Entry Name FTSZ_MYCTU - General References
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Sureka K, Hossain T, Mukherjee P, Chatterjee P, Datta P, Kundu M, Basu J: Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division. PLoS One. 2010 Jan 6;5(1):e8590. doi: 10.1371/journal.pone.0008590. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Leung AK, Lucile White E, Ross LJ, Reynolds RC, DeVito JA, Borhani DW: Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches. J Mol Biol. 2004 Sep 17;342(3):953-70. [Article]
- Respicio L, Nair PA, Huang Q, Anil B, Tracz S, Truglio JJ, Kisker C, Raleigh DP, Ojima I, Knudson DL, Tonge PJ, Slayden RA: Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinb). 2008 Sep;88(5):420-9. doi: 10.1016/j.tube.2008.03.001. Epub 2008 May 13. [Article]
- Li Y, Hsin J, Zhao L, Cheng Y, Shang W, Huang KC, Wang HW, Ye S: FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation. Science. 2013 Jul 26;341(6144):392-5. doi: 10.1126/science.1239248. [Article]