Cell division protein ZipA

Details

Name
Cell division protein ZipA
Synonyms
  • FtsZ interacting protein A
Gene Name
zipA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012789|Cell division protein ZipA
MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDD
EGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPH
PAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAE
PAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGP
ALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVV
LDDQRRMMTPQKLREYQDIIREVKDANA
Number of residues
328
Molecular Weight
36475.105
Theoretical pI
5.88
GO Classification
Processes
barrier septum assembly / FtsZ-dependent cytokinesis
Components
cell division site / integral component of plasma membrane / plasma membrane
General Function
Not Available
Specific Function
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring (PubMed:9008158, PubMed:11847116, PubMed:22164258, PubMed:22304478, PubMed:23233671). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL and FtsN (PubMed:11847116, PubMed:11948172). ZipA overproduction protects FtsZ from degradation by ClpP by preventing recognition by ClpX (PubMed:23233671). Does not affect the GTPase activity of FtsZ (PubMed:10209756).
Pfam Domain Function
Transmembrane Regions
7-27
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0012790|Cell division protein ZipA (zipA)
ATGATGCAGGATTTGCGTCTGATATTAATCATTGTTGGCGCGATCGCCATAATCGCTTTA
CTGGTACATGGTTTCTGGACCAGCCGTAAAGAACGATCTTCTATGTTCCGCGATCGGCCA
TTAAAACGAATGAAGTCAAAACGTGACGACGATTCTTATGACGAGGATGTCGAAGATGAT
GAGGGCGTTGGTGAGGTTCGTGTTCACCGCGTGAATCATGCCCCGGCTAACGCTCAGGAG
CATGAGGCTGCTCGTCCGTCGCCGCAACACCAGTACCAACCGCCTTATGCGTCTGCGCAG
CCGCGTCAACCGGTCCAGCAGCCGCCTGAAGCGCAGGTACCGCCGCAACATGCTCCGCAT
CCAGCGCAGCCGGTGCAGCAGCCTGCCTATCAGCCGCAGCCTGAACAGCCGTTGCAGCAG
CCAGTTTCGCCACAGGTCGCGCCAGCGCCGCAGCCTGTGCATTCAGCACCGCAACCGGCA
CAACAGGCTTTCCAGCCTGCAGAACCCGTAGCGGCACCACAGCCTGAGCCTGTAGCGGAA
CCTGCTCCAGTTATGGATAAACCGAAGCGCAAAGAAGCGGTGATTATCATGAACGTCGCG
GCGCATCACGGTAGCGAGCTAAACGGTGAACTGCTTCTTAACAGCATTCAACAAGCGGGC
TTCATTTTTGGCGATATGAATATTTACCATCGTCATCTTAGCCCGGATGGCAGCGGCCCG
GCGTTATTCAGCCTGGCGAATATGGTGAAACCGGGAACCTTTGATCCTGAAATGAAGGAT
TTCACTACTCCGGGTGTCACTATCTTTATGCAGGTACCGTCTTACGGTGACGAGCTGCAG
AACTTCAAGCTGATGCTGCAATCTGCGCAGCATATTGCCGATGAAGTGGGCGGTGTCGTG
CTTGACGATCAGCGCCGTATGATGACTCCGCAGAAATTGCGCGAGTACCAGGACATCATC
CGCGAAGTCAAAGACGCCAACGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP77173
UniProtKB Entry NameZIPA_ECOLI
GenBank Protein ID1816522
GenBank Gene IDU74650
General References
  1. Hale CA, de Boer PA: Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell. 1997 Jan 24;88(2):175-85. [Article]
  2. Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Hale CA, de Boer PA: Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA. J Bacteriol. 1999 Jan;181(1):167-76. [Article]
  6. Liu Z, Mukherjee A, Lutkenhaus J: Recruitment of ZipA to the division site by interaction with FtsZ. Mol Microbiol. 1999 Mar;31(6):1853-61. [Article]
  7. Pichoff S, Lutkenhaus J: Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J. 2002 Feb 15;21(4):685-93. [Article]
  8. Hale CA, de Boer PA: ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli. J Bacteriol. 2002 May;184(9):2552-6. [Article]
  9. Ohashi T, Hale CA, de Boer PA, Erickson HP: Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain. J Bacteriol. 2002 Aug;184(15):4313-5. [Article]
  10. Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO: Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005 Oct 14;280(41):34409-19. Epub 2005 Aug 3. [Article]
  11. Davies BW, Kohanski MA, Simmons LA, Winkler JA, Collins JJ, Walker GC: Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli. Mol Cell. 2009 Dec 11;36(5):845-60. doi: 10.1016/j.molcel.2009.11.024. [Article]
  12. Kuchibhatla A, Bhattacharya A, Panda D: ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments. PLoS One. 2011;6(12):e28262. doi: 10.1371/journal.pone.0028262. Epub 2011 Dec 2. [Article]
  13. Skoog K, Daley DO: The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ. Biochemistry. 2012 Feb 21;51(7):1407-15. doi: 10.1021/bi2015647. Epub 2012 Feb 9. [Article]
  14. Pazos M, Natale P, Vicente M: A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J Biol Chem. 2013 Feb 1;288(5):3219-26. doi: 10.1074/jbc.M112.434944. Epub 2012 Dec 11. [Article]
  15. Moy FJ, Glasfeld E, Mosyak L, Powers R: Solution structure of ZipA, a crucial component of Escherichia coli cell division. Biochemistry. 2000 Aug 8;39(31):9146-56. [Article]
  16. Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, Seehra J, Somers WS: The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J. 2000 Jul 3;19(13):3179-91. [Article]
  17. Jennings LD, Foreman KW, Rush TS 3rd, Tsao DH, Mosyak L, Li Y, Sukhdeo MN, Ding W, Dushin EG, Kenny CH, Moghazeh SL, Petersen PJ, Ruzin AV, Tuckman M, Sutherland AG: Design and synthesis of indolo[2,3-a]quinolizin-7-one inhibitors of the ZipA-FtsZ interaction. Bioorg Med Chem Lett. 2004 Mar 22;14(6):1427-31. [Article]
  18. Rush TS 3rd, Grant JA, Mosyak L, Nicholls A: A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction. J Med Chem. 2005 Mar 10;48(5):1489-95. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04154N-Methyl-N-[3-(6-Phenyl[1,2,4]Triazolo[4,3-B]Pyridazin-3-Yl)Phenyl]AcetamideexperimentalunknownDetails
DB02191(7as,12ar,12bs)-1,2,3,4,7a,12,12a,12b-Octahydroindolo[2,3-a]Quinolizin-7(6h)-OneexperimentalunknownDetails
DB01967N-{3-[(7ar,12as,12bs)-7-Oxo-1,3,4,6,7,7a,12a,12b-Octahydroindolo[2,3-a]Quinolizin-12(2h)-Yl]Propyl}Propane-2-SulfonamideexperimentalunknownDetails
DB039164-{2-[4-(2-Aminoethyl)Piperazin-1-Yl]Pyridin-4-Yl}-N-(3-Chloro-4-Methylphenyl)Pyrimidin-2-AmineexperimentalunknownDetails