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Protein

Cell division protein ZapA

Gene

zapA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

GO - Biological processi

  • barrier septum assembly Source: EcoliWiki
  • cell division Source: EcoliWiki
  • FtsZ-dependent cytokinesis Source: EcoCyc
  • septin ring assembly Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Enzyme and pathway databases

BioCyciEcoCyc:EG12878-MONOMER.
ECOL316407:JW2878-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein ZapA
Alternative name(s):
Z ring-associated protein ZapA
Gene namesi
Name:zapA
Synonyms:ygfE
Ordered Locus Names:b2910, JW2878
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12878. zapA.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Localizes at mid-cell.

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • cell septum Source: EcoliWiki
  • cytosol Source: EcoCyc
  • plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 109109Cell division protein ZapAPRO_0000169350Add
BLAST

Proteomic databases

EPDiP0ADS2.
PaxDbiP0ADS2.
PRIDEiP0ADS2.

Interactioni

Subunit structurei

Homodimer. Interacts with FtsZ.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
zapBP0AF364EBI-1119901,EBI-1134093

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262169. 354 interactions.
IntActiP0ADS2. 8 interactions.
STRINGi511145.b2910.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi13 – 186Combined sources
Helixi21 – 233Combined sources
Helixi24 – 4522Combined sources
Helixi50 – 10152Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P1MX-ray1.95A/B1-109[»]
ProteinModelPortaliP0ADS2.
SMRiP0ADS2. Positions 4-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili21 – 9979Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the ZapA family. Type 1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4107YUN. Bacteria.
COG3027. LUCA.
HOGENOMiHOG000263522.
InParanoidiP0ADS2.
KOiK09888.
OMAiNICYELH.
OrthoDBiEOG69SKDP.
PhylomeDBiP0ADS2.

Family and domain databases

HAMAPiMF_02012. ZapA_type1.
InterProiIPR007838. Cell_div_ZapA-like.
IPR023771. Cell_div_ZapA_eubact.
[Graphical view]
PfamiPF05164. ZapA. 1 hit.
[Graphical view]
SUPFAMiSSF102829. SSF102829. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ADS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAQPVDIQI FGRSLRVNCP PDQRDALNQA ADDLNQRLQD LKERTRVTNT
60 70 80 90 100
EQLVFIAALN ISYELAQEKA KTRDYAASME QRIRMLQQTI EQALLEQGRI

TEKTNQNFE
Length:109
Mass (Da):12,594
Last modified:December 6, 2005 - v1
Checksum:i26777CC2B2B71148
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141S → Y (PubMed:1339425).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28377 Genomic DNA. Translation: AAA69078.1.
U00096 Genomic DNA. Translation: AAC75948.1.
AP009048 Genomic DNA. Translation: BAE76975.1.
D90281 Genomic DNA. No translation available.
M12965 Genomic DNA. No translation available.
PIRiF65075.
RefSeqiNP_417386.1. NC_000913.3.
WP_001276008.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75948; AAC75948; b2910.
BAE76975; BAE76975; BAE76975.
GeneIDi947404.
KEGGiecj:JW2878.
eco:b2910.
PATRICi32121234. VBIEscCol129921_3005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28377 Genomic DNA. Translation: AAA69078.1.
U00096 Genomic DNA. Translation: AAC75948.1.
AP009048 Genomic DNA. Translation: BAE76975.1.
D90281 Genomic DNA. No translation available.
M12965 Genomic DNA. No translation available.
PIRiF65075.
RefSeqiNP_417386.1. NC_000913.3.
WP_001276008.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P1MX-ray1.95A/B1-109[»]
ProteinModelPortaliP0ADS2.
SMRiP0ADS2. Positions 4-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262169. 354 interactions.
IntActiP0ADS2. 8 interactions.
STRINGi511145.b2910.

Proteomic databases

EPDiP0ADS2.
PaxDbiP0ADS2.
PRIDEiP0ADS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75948; AAC75948; b2910.
BAE76975; BAE76975; BAE76975.
GeneIDi947404.
KEGGiecj:JW2878.
eco:b2910.
PATRICi32121234. VBIEscCol129921_3005.

Organism-specific databases

EchoBASEiEB2716.
EcoGeneiEG12878. zapA.

Phylogenomic databases

eggNOGiENOG4107YUN. Bacteria.
COG3027. LUCA.
HOGENOMiHOG000263522.
InParanoidiP0ADS2.
KOiK09888.
OMAiNICYELH.
OrthoDBiEOG69SKDP.
PhylomeDBiP0ADS2.

Enzyme and pathway databases

BioCyciEcoCyc:EG12878-MONOMER.
ECOL316407:JW2878-MONOMER.

Miscellaneous databases

PROiP0ADS2.

Family and domain databases

HAMAPiMF_02012. ZapA_type1.
InterProiIPR007838. Cell_div_ZapA-like.
IPR023771. Cell_div_ZapA_eubact.
[Graphical view]
PfamiPF05164. ZapA. 1 hit.
[Graphical view]
SUPFAMiSSF102829. SSF102829. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "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."
    Nakahigashi K., Miyamoto K., Nishimura K., Inokuchi H.
    J. Bacteriol. 174:7352-7359(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-105.
    Strain: ATCC 33694 / HB101.
  4. "Escherichia coli 6S RNA gene is part of a dual-function transcription unit."
    Hsu L.M., Zagorski J., Wang Z., Fournier M.J.
    J. Bacteriol. 161:1162-1170(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-109.
  5. "Detection of new genes in a bacterial genome using Markov models for three gene classes."
    Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.
    Nucleic Acids Res. 23:3554-3562(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ."
    Gueiros-Filho F.J., Losick R.
    Genes Dev. 16:2544-2556(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli."
    Johnson J.E., Lackner L.L., Hale C.A., de Boer P.A.J.
    J. Bacteriol. 186:2418-2429(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN THE RECRUITMENT OF OTHER CELL DIVISION PROTEINS.
  8. "Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins."
    Anderson D.E., Gueiros-Filho F.J., Erickson H.P.
    J. Bacteriol. 186:5775-5781(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSZ.
  9. "Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli."
    Goehring N.W., Gueiros-Filho F., Beckwith J.
    Genes Dev. 19:127-137(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF THE SEPTAL RECRUITMENT PATHWAY.
  10. Cited for: TIMING OF RECRUITMENT DURING CELL DIVISION.
  11. "Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly."
    Goehring N.W., Gonzalez M.D., Beckwith J.
    Mol. Microbiol. 61:33-45(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY OF CELL DIVISION COMPONENTS.
  12. "FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP."
    Small E., Marrington R., Rodger A., Scott D.J., Sloan K., Roper D., Dafforn T.R., Addinall S.G.
    J. Mol. Biol. 369:210-221(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION OF FTSZ GTPASE ACTIVITY, INTERACTION WITH FTSZ, SUBUNIT.
    Strain: K12 / MG1655 / ATCC 47076.
  13. "Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli."
    Addinall S.G., Johnson K.A., Dafforn T., Smith C., Rodger A., Gomez R.P., Sloan K., Blewett A., Scott D.J., Roper D.I.
    Acta Crystallogr. F 61:305-307(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiZAPA_ECOLI
AccessioniPrimary (citable) accession number: P0ADS2
Secondary accession number(s): P45580, Q2M9T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 13, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.