Cell division protein ZipA
Details
- Name
- Cell division protein ZipA
- Kind
- protein
- Synonyms
- FtsZ interacting protein A
- Gene Name
- zipA
- UniProtKB Entry
- P77173Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Processesbarrier septum assembly / FtsZ-dependent cytokinesisComponentscell division site / integral component of plasma membrane / plasma membrane
- General 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:11847116, PubMed:22164258, PubMed:22304478, PubMed:23233671, PubMed:9008158). 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).
- Specific Function
- protein homodimerization activity
- Pfam Domain Function
- ZipA_C (PF04354)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P77173 UniProtKB Entry Name ZIPA_ECOLI GenBank Protein ID 1816522 GenBank Gene ID U74650 PDB ID(s) 1F46, 1F47, 1F7W, 1F7X, 1S1J, 1S1S, 1Y2F, 1Y2G KEGG ID ecj:JW2404 NCBI Gene ID 946869 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-Methyl-N-[3-(6-Phenyl[1,2,4]Triazolo[4,3-B]Pyridazin-3-Yl)Phenyl]Acetamide experimental unknown target Details (7as,12ar,12bs)-1,2,3,4,7a,12,12a,12b-Octahydroindolo[2,3-a]Quinolizin-7(6h)-One experimental unknown target Details N-{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-Sulfonamide experimental unknown target Details 4-{2-[4-(2-Aminoethyl)Piperazin-1-Yl]Pyridin-4-Yl}-N-(3-Chloro-4-Methylphenyl)Pyrimidin-2-Amine experimental unknown target Details