Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Protein: cell division factor ZapA, localizes to the cytokinetic ring



Gene: zapA Accession Numbers: EG12878 (EcoCyc), b2910, ECK2905

Synonyms: ygfE

Regulation Summary Diagram: ?

Subunit composition of cell division factor ZapA, localizes to the cytokinetic ring = [ZapA]4
         cell division factor ZapA, localizes to the cytokinetic ring = ZapA

Summary:
ZapA binds to FtsZ polymers [Small07] and promotes the coherence of the Z-ring by cross-linking FtsZ polymers and stabilizing longitudinal interactions between FtsZ molecules [Dajkovic10]. This effect is counteracted by ZapB [Galli12].

Before septum formation, a complex of the early-division proteins ZipA, ZapA, and ZapB oscillates along the cell with a periodicity that is opposite that of MinC. The oscillation is dependent on the presence of FtsZ filaments and on the Min system [Bisicchia13].

During growth in minimal medium, ZapA and FtsZ are present at approximately equimolar concentration [Mohammadi09]. ZapA was reported to be a potent inhibitor of the GTPase activity of FtsZ [Small07], but later experiments with ZapA lacking a His tag found little effect of ZapA on FtsZ GTPase activity [Mohammadi09]. [Galli12] found that inhibition of the GTPase activity of FtsZ by ZapA was stronger at pH 6.5 than at pH 7.5; at the higher pH, addition of ZapB further weakened the effect.

ZapA localizes to the cell division site, but is not essential [GueirosFilho02]. It is not required for targeting of the MinC/MinD complex to the Z-ring [Johnson04], but is required for recruiting ZapB to the Z-ring [Galli10]. ZapA also interacts with FtsI and FtsN [Alexeeva10] and indirectly, via FtsZ, with ZipA [Pazos13]. FtsZ and ZapA disassemble from the cell division site before the constriction of the inner membrane is complete and the cytoplasm is separated [Soderstrom14].

A preliminary analysis of the crystal structure of ZapA has been published [Addinall05], and a crystal structure has been solved at 1.95 Å resolution [Roach14]. ZapA consists of two domains; the N-terminal globular domain is required for interaction with FtsZ, while the C-terminal coiled-coil domain is required for interaction with ZapB and for homodimerization [Galli12]. ZapA exists in a dimer/tetramer equilibrium in solution [Small07]. An I83E mutant is a constitutive dimer that is able to bind to FtsZ, but is unable to induce FtsZ bundling [PachecoGomez13]. Residues that are involved in the interaction with FtsZ and in filament bundling were identified by site-directed mutagenesis [Roach14].

A zapA deletion strain has a cytokinesis defect [Mohammadi09, Dajkovic10, Buss13]. Reports disagree on whether [Dajkovic10] or not [Mohammadi09] His-tagged ZapA can complement the defect. A zapA mutant has an abnormal cell division septum; single-molecule based superresolution imaging shows a disordered arrangement of FtsZ clusters [Buss13]. Overproduction of ZapA results in aberrant localization of FtsZ and ZapB and the formation of elongated cells [Galli12].

ZapA: "Z-ring-associated protein A" [GueirosFilho02]

Reviews: [Vicente06, Weiss04, Margolin03]

Citations: [Abe13]

Locations: cytosol

Map Position: [3,053,634 -> 3,053,963] (65.82 centisomes)
Length: 330 bp / 109 aa

Molecular Weight of Polypeptide: 12.594 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009554 , EchoBASE:EB2716 , EcoGene:EG12878 , EcoliWiki:b2910 , ModBase:P0ADS2 , OU-Microarray:b2910 , PortEco:zapA , PR:PRO_000024245 , Pride:P0ADS2 , Protein Model Portal:P0ADS2 , RefSeq:NP_417386 , RegulonDB:EG12878 , SMR:P0ADS2 , String:511145.b2910 , UniProt:P0ADS2

Relationship Links: InterPro:IN-FAMILY:IPR007838 , InterPro:IN-FAMILY:IPR023771 , PDB:Structure:4P1M , Pfam:IN-FAMILY:PF05164

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0000917 - barrier septum assembly Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Galli10]
GO:0000921 - septin ring assembly Inferred from experiment [Goehring05]
GO:0043093 - FtsZ-dependent cytokinesis Inferred from experiment [Dajkovic10, Mohammadi09]
GO:0051301 - cell division Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Galli10, Small07]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Galli12, Alexeeva10, Small07, Galli10]
GO:0042802 - identical protein binding Inferred from experiment [Alexeeva10]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08]
GO:0030428 - cell septum Inferred from experiment [Galli10]
GO:0032153 - cell division site Inferred from experiment [Goehring05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: cell processes cell division

Essentiality data for zapA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Created 19-Apr-2007 by Keseler I , SRI International
Last-Curated ? 16-Jul-2014 by Keseler I , SRI International


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 14
[Nakahigashi92, UniProt10a]
Alternate sequence: S → Y; UniProt: (in Ref. 3);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
10/20/97 Gene b2910 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12878; confirmed by SwissProt match.


References

Abe13: Abe A, Furukawa S, Migita Y, Tanaka M, Ogihara H, Morinaga Y (2013). "Sublethal high hydrostatic pressure treatment reveals the importance of genes coding cytoskeletal protein in Escherichia coli morphogenesis." Curr Microbiol 67(5);515-21. PMID: 23708427

Addinall05: Addinall SG, Johnson KA, Dafforn T, Smith C, Rodger A, Gomez RP, Sloan K, Blewett A, Scott DJ, Roper DI (2005). "Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli." Acta Crystallograph Sect F Struct Biol Cryst Commun 61(Pt 3);305-7. PMID: 16511026

Alexeeva10: Alexeeva S, Gadella TW, Verheul J, Verhoeven GS, den Blaauwen T (2010). "Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET." Mol Microbiol 77(2);384-98. PMID: 20497333

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bisicchia13: Bisicchia P, Arumugam S, Schwille P, Sherratt D (2013). "MinC, MinD, and MinE drive counter-oscillation of early-cell-division proteins prior to Escherichia coli septum formation." MBio 4(6);e00856-13. PMID: 24327341

Buss13: Buss J, Coltharp C, Huang T, Pohlmeyer C, Wang SC, Hatem C, Xiao J (2013). "In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy." Mol Microbiol 89(6);1099-120. PMID: 23859153

Dajkovic10: Dajkovic A, Pichoff S, Lutkenhaus J, Wirtz D (2010). "Cross-linking FtsZ polymers into coherent Z rings." Mol Microbiol 78(3);651-68. PMID: 20969647

Galli10: Galli E, Gerdes K (2010). "Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring." Mol Microbiol 76(6);1514-26. PMID: 20487275

Galli12: Galli E, Gerdes K (2012). "FtsZ-ZapA-ZapB interactome of Escherichia coli." J Bacteriol 194(2);292-302. PMID: 22056926

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Goehring05: Goehring NW, Gueiros-Filho F, Beckwith J (2005). "Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli." Genes Dev 19(1);127-37. PMID: 15630023

GueirosFilho02: Gueiros-Filho FJ, Losick R (2002). "A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ." Genes Dev 16(19);2544-56. PMID: 12368265

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Johnson04: Johnson JE, Lackner LL, Hale CA, de Boer PA (2004). "ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli." J Bacteriol 186(8);2418-29. PMID: 15060045

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Margolin03: Margolin W (2003). "Bacterial division: the fellowship of the ring." Curr Biol 13(1);R16-8. PMID: 12526758

Mohammadi09: Mohammadi T, Ploeger GE, Verheul J, Comvalius AD, Martos A, Alfonso C, van Marle J, Rivas G, den Blaauwen T (2009). "The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro." Biochemistry 48(46);11056-66. PMID: 19842714

Nakahigashi92: Nakahigashi K, Miyamoto K, Nishimura K, Inokuchi H (1992). "Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone." J Bacteriol 1992;174(22);7352-9. PMID: 1339425

PachecoGomez13: Pacheco-Gomez R, Cheng X, Hicks MR, Smith CJ, Roper DI, Addinall S, Rodger A, Dafforn TR (2013). "Tetramerization of ZapA is required for FtsZ bundling." Biochem J 449(3);795-802. PMID: 23098212

Pazos13: Pazos M, Natale P, Margolin W, Vicente M (2013). "Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation." Environ Microbiol 15(12);3282-91. PMID: 23957637

Roach14: Roach EJ, Kimber MS, Khursigara CM (2014). "Crystal structure and site-directed mutational analysis reveals key residues involved in Escherichia coli ZapA function." J Biol Chem. PMID: 25002581

Serres01: Serres MH, Gopal S, Nahum LA, Liang P, Gaasterland T, Riley M (2001). "A functional update of the Escherichia coli K-12 genome." Genome Biol 2(9);RESEARCH0035. PMID: 11574054

Small07: Small E, Marrington R, Rodger A, Scott DJ, Sloan K, Roper D, Dafforn TR, Addinall SG (2007). "FtsZ Polymer-bundling by the Escherichia coli ZapA Orthologue, YgfE, Involves a Conformational Change in Bound GTP." J Mol Biol 369(1):210-21. PMID: 17428494

Soderstrom14: Soderstrom B, Skoog K, Blom H, Weiss DS, von Heijne G, Daley DO (2014). "Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization." Mol Microbiol 92(1);1-9. PMID: 24506818

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Vicente06: Vicente M, Rico AI (2006). "The order of the ring: assembly of Escherichia coli cell division components." Mol Microbiol 61(1);5-8. PMID: 16824090

Weiss04: Weiss DS (2004). "Bacterial cell division and the septal ring." Mol Microbiol 54(3);588-97. PMID: 15491352


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, biocyc14.