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Protein

Cell division protein ZipA

Gene

zipA

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

Functioni

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).7 Publications

GO - Biological processi

  • barrier septum assembly Source: EcoliWiki
  • FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Enzyme and pathway databases

BioCyciEcoCyc:G7258-MONOMER.
ECOL316407:JW2404-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein ZipAUniRule annotation
Alternative name(s):
FtsZ interacting protein A1 Publication
Gene namesi
Name:zipA1 PublicationUniRule annotation
Ordered Locus Names:b2412, JW2404
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14169. zipA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66PeriplasmicUniRule annotation1 Publication
Transmembranei7 – 2721HelicalUniRule annotationAdd
BLAST
Topological domaini28 – 328301CytoplasmicUniRule annotation1 PublicationAdd
BLAST

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • integral component of plasma membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3954.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Cell division protein ZipAPRO_0000214521Add
BLAST

Proteomic databases

PaxDbiP77173.
PRIDEiP77173.

Expressioni

Inductioni

Repressed 1.5-fold by hydroxyurea.1 Publication

Interactioni

Subunit structurei

Interacts with FtsZ via their C-terminal domains (PubMed:9008158, PubMed:10209756, PubMed:10880432, PubMed:22164258). Can form homodimers prior to association with FtsZ (PubMed:22304478).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ftsZP0A9A64EBI-1029213,EBI-370963

Protein-protein interaction databases

BioGridi4261708. 552 interactions.
DIPiDIP-1157N.
IntActiP77173. 2 interactions.
MINTiMINT-89938.
STRINGi511145.b2412.

Chemistry

BindingDBiP77173.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi193 – 2008Combined sources
Helixi209 – 21810Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 2273Combined sources
Beta strandi228 – 2347Combined sources
Beta strandi241 – 2499Combined sources
Turni256 – 2594Combined sources
Beta strandi262 – 27211Combined sources
Beta strandi274 – 2763Combined sources
Helixi278 – 29619Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi305 – 3073Combined sources
Helixi310 – 32617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F46X-ray1.50A/B189-328[»]
1F47X-ray1.95B185-328[»]
1F7WNMR-A185-328[»]
1F7XNMR-A185-328[»]
1S1JX-ray2.18A/B185-328[»]
1S1SX-ray2.10A/B185-328[»]
1Y2FX-ray2.00A190-328[»]
1Y2GX-ray1.90A/B189-328[»]
DisProtiDP00161.
ProteinModelPortaliP77173.
SMRiP77173. Positions 189-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77173.

Family & Domainsi

Domaini

Contains an N-terminal transmembrane domain, followed by a charged domain, an unstructured P/Q domain rich in proline and glutamine, and a C-terminal FtsZ-binding domain.1 Publication

Sequence similaritiesi

Belongs to the ZipA family.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107NPY. Bacteria.
COG3115. LUCA.
HOGENOMiHOG000274007.
InParanoidiP77173.
KOiK03528.
OMAiLPCYGEA.
OrthoDBiEOG6X10VC.

Family and domain databases

Gene3Di3.30.1400.10. 1 hit.
HAMAPiMF_00509. ZipA.
InterProiIPR011919. Cell_div_ZipA.
IPR007449. ZipA_FtsZ-bd_C.
[Graphical view]
PfamiPF04354. ZipA_C. 1 hit.
[Graphical view]
ProDomiPD035754. ZipA_Fts_Z_bd_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00771. ZipA_C. 1 hit.
[Graphical view]
SUPFAMiSSF64383. SSF64383. 1 hit.
TIGRFAMsiTIGR02205. septum_zipA. 1 hit.

Sequencei

Sequence statusi: Complete.

P77173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD
60 70 80 90 100
DSYDEDVEDD EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ
110 120 130 140 150
PRQPVQQPPE AQVPPQHAPH PAQPVQQPAY QPQPEQPLQQ PVSPQVAPAP
160 170 180 190 200
QPVHSAPQPA QQAFQPAEPV AAPQPEPVAE PAPVMDKPKR KEAVIIMNVA
210 220 230 240 250
AHHGSELNGE LLLNSIQQAG FIFGDMNIYH RHLSPDGSGP ALFSLANMVK
260 270 280 290 300
PGTFDPEMKD FTTPGVTIFM QVPSYGDELQ NFKLMLQSAQ HIADEVGGVV
310 320
LDDQRRMMTP QKLREYQDII REVKDANA
Length:328
Mass (Da):36,475
Last modified:August 29, 2003 - v3
Checksum:iA20F119A153A782B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111L → A in AAB42061 (PubMed:9008158).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U74650 Genomic DNA. Translation: AAB42061.1.
U00096 Genomic DNA. Translation: AAC75465.1.
AP009048 Genomic DNA. Translation: BAA16284.1.
PIRiC65015.
RefSeqiNP_416907.1. NC_000913.3.
WP_001300494.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75465; AAC75465; b2412.
BAA16284; BAA16284; BAA16284.
GeneIDi946869.
KEGGiecj:JW2404.
eco:b2412.
PATRICi32120207. VBIEscCol129921_2506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U74650 Genomic DNA. Translation: AAB42061.1.
U00096 Genomic DNA. Translation: AAC75465.1.
AP009048 Genomic DNA. Translation: BAA16284.1.
PIRiC65015.
RefSeqiNP_416907.1. NC_000913.3.
WP_001300494.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F46X-ray1.50A/B189-328[»]
1F47X-ray1.95B185-328[»]
1F7WNMR-A185-328[»]
1F7XNMR-A185-328[»]
1S1JX-ray2.18A/B185-328[»]
1S1SX-ray2.10A/B185-328[»]
1Y2FX-ray2.00A190-328[»]
1Y2GX-ray1.90A/B189-328[»]
DisProtiDP00161.
ProteinModelPortaliP77173.
SMRiP77173. Positions 189-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261708. 552 interactions.
DIPiDIP-1157N.
IntActiP77173. 2 interactions.
MINTiMINT-89938.
STRINGi511145.b2412.

Chemistry

BindingDBiP77173.
ChEMBLiCHEMBL3954.

Proteomic databases

PaxDbiP77173.
PRIDEiP77173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75465; AAC75465; b2412.
BAA16284; BAA16284; BAA16284.
GeneIDi946869.
KEGGiecj:JW2404.
eco:b2412.
PATRICi32120207. VBIEscCol129921_2506.

Organism-specific databases

EchoBASEiEB3921.
EcoGeneiEG14169. zipA.

Phylogenomic databases

eggNOGiENOG4107NPY. Bacteria.
COG3115. LUCA.
HOGENOMiHOG000274007.
InParanoidiP77173.
KOiK03528.
OMAiLPCYGEA.
OrthoDBiEOG6X10VC.

Enzyme and pathway databases

BioCyciEcoCyc:G7258-MONOMER.
ECOL316407:JW2404-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP77173.
PROiP77173.

Family and domain databases

Gene3Di3.30.1400.10. 1 hit.
HAMAPiMF_00509. ZipA.
InterProiIPR011919. Cell_div_ZipA.
IPR007449. ZipA_FtsZ-bd_C.
[Graphical view]
PfamiPF04354. ZipA_C. 1 hit.
[Graphical view]
ProDomiPD035754. ZipA_Fts_Z_bd_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00771. ZipA_C. 1 hit.
[Graphical view]
SUPFAMiSSF64383. SSF64383. 1 hit.
TIGRFAMsiTIGR02205. septum_zipA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli."
    Hale C.A., de Boer P.A.J.
    Cell 88:175-185(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, TOPOLOGY.
    Strain: PB103.
  2. "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."
    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., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA."
    Hale C.A., de Boer P.A.
    J. Bacteriol. 181:167-176(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Recruitment of ZipA to the division site by interaction with FtsZ."
    Liu Z., Mukherjee A., Lutkenhaus J.
    Mol. Microbiol. 31:1853-1861(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION.
    Strain: K12.
  7. "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli."
    Pichoff S., Lutkenhaus J.
    EMBO J. 21:685-693(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN Z RING ASSEMBLY, FUNCTION IN RECRUITMENT OF FTSK.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli."
    Hale C.A., de Boer P.A.J.
    J. Bacteriol. 184:2552-2556(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF CELL DIVISION PROTEINS.
  9. "Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain."
    Ohashi T., Hale C.A., de Boer P.A., Erickson H.P.
    J. Bacteriol. 184:4313-4315(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  10. Cited for: SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  11. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYDROXYUREA.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments."
    Kuchibhatla A., Bhattacharya A., Panda D.
    PLoS ONE 6:E28262-E28262(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FTSZ.
  13. "The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ."
    Skoog K., Daley D.O.
    Biochemistry 51:1407-1415(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
    Strain: K12 / MG1655 / ATCC 47076.
  14. "A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein."
    Pazos M., Natale P., Vicente M.
    J. Biol. Chem. 288:3219-3226(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Solution structure of ZipA, a crucial component of Escherichia coli cell division."
    Moy F.J., Glasfeld E., Mosyak L., Powers R.
    Biochemistry 39:9146-9156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 185-328.
  16. "The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography."
    Mosyak L., Zhang Y., Glasfeld E., Haney S., Stahl M., Seehra J., Somers W.S.
    EMBO J. 19:3179-3191(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 189-328, INTERACTION WITH FTSZ.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 185-328.
  18. "A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction."
    Rush T.S. III, Grant J.A., Mosyak L., Nicholls A.
    J. Med. Chem. 48:1489-1495(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 189-328.

Entry informationi

Entry nameiZIPA_ECOLI
AccessioniPrimary (citable) accession number: P77173
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 29, 2003
Last modified: April 13, 2016
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has been isolated as a 91 kDa complex containing ZipA-EptA and an unidentified 24 kDa protein (PubMed:16079137), but it was shown later that there is no physical interaction between ZipA and EptA (PubMed:22304478).2 Publications

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.