UniProt: ZAPA

Database: UniProt
Entry: ZAPA_ECOLI

LinkDB:  ZAPA_ECOLI 
Original site:  ZAPA_ECOLI

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Ontology (9)   
   GO (9)   
Gene (4)   
   KEGG GENES (2)   
   NCBI-Gene (2)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (5)   
   EMBL (5)   
3D Structure (1)   
   PDB (1)   
Protein domain (5)   
   InterPro (4)   
   Pfam (1)   
Literature (13)   
   PubMed (13)   
All databases (39)   

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ID   ZAPA_ECOLI              Reviewed;         109 AA.
AC   P0ADS2; P45580; Q2M9T1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=Cell division protein ZapA;
DE   AltName: Full=Z ring-associated protein ZapA;
GN   Name=zapA; Synonyms=ygfE; OrderedLocusNames=b2910, JW2878;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-105.
RC   STRAIN=ATCC 33694 / HB101;
RX   PubMed=1339425; DOI=10.1128/jb.174.22.7352-7359.1992;
RA   Nakahigashi K., Miyamoto K., Nishimura K., Inokuchi H.;
RT   "Isolation and characterization of a light-sensitive mutant of Escherichia
RT   coli K-12 with a mutation in a gene that is required for the biosynthesis
RT   of ubiquinone.";
RL   J. Bacteriol. 174:7352-7359(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-109.
RX   PubMed=2579060; DOI=10.1128/jb.161.3.1162-1170.1985;
RA   Hsu L.M., Zagorski J., Wang Z., Fournier M.J.;
RT   "Escherichia coli 6S RNA gene is part of a dual-function transcription
RT   unit.";
RL   J. Bacteriol. 161:1162-1170(1985).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA   Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT   "Detection of new genes in a bacterial genome using Markov models for three
RT   gene classes.";
RL   Nucleic Acids Res. 23:3554-3562(1995).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12368265; DOI=10.1101/gad.1014102;
RA   Gueiros-Filho F.J., Losick R.;
RT   "A widely conserved bacterial cell division protein that promotes assembly
RT   of the tubulin-like protein FtsZ.";
RL   Genes Dev. 16:2544-2556(2002).
RN   [7]
RP   ROLE IN THE RECRUITMENT OF OTHER CELL DIVISION PROTEINS.
RX   PubMed=15060045; DOI=10.1128/jb.186.8.2418-2429.2004;
RA   Johnson J.E., Lackner L.L., Hale C.A., de Boer P.A.J.;
RT   "ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD,
RT   complexes to septal ring assemblies in Escherichia coli.";
RL   J. Bacteriol. 186:2418-2429(2004).
RN   [8]
RP   INTERACTION WITH FTSZ.
RX   PubMed=15317782; DOI=10.1128/jb.186.17.5775-5781.2004;
RA   Anderson D.E., Gueiros-Filho F.J., Erickson H.P.;
RT   "Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli
RT   and effects of FtsZ-regulating proteins.";
RL   J. Bacteriol. 186:5775-5781(2004).
RN   [9]
RP   COMPONENT OF THE SEPTAL RECRUITMENT PATHWAY.
RX   PubMed=15630023; DOI=10.1101/gad.1253805;
RA   Goehring N.W., Gueiros-Filho F., Beckwith J.;
RT   "Premature targeting of a cell division protein to midcell allows
RT   dissection of divisome assembly in Escherichia coli.";
RL   Genes Dev. 19:127-137(2005).
RN   [10]
RP   TIMING OF RECRUITMENT DURING CELL DIVISION.
RX   PubMed=15752189; DOI=10.1111/j.1365-2958.2005.04502.x;
RA   Aarsman M.E.G., Piette A., Fraipont C., Vinkenvleugel T.M.F.,
RA   Nguyen-Disteche M., den Blaauwen T.;
RT   "Maturation of the Escherichia coli divisome occurs in two steps.";
RL   Mol. Microbiol. 55:1631-1645(2005).
RN   [11]
RP   ASSEMBLY OF CELL DIVISION COMPONENTS.
RX   PubMed=16824093; DOI=10.1111/j.1365-2958.2006.05206.x;
RA   Goehring N.W., Gonzalez M.D., Beckwith J.;
RT   "Premature targeting of cell division proteins to midcell reveals
RT   hierarchies of protein interactions involved in divisome assembly.";
RL   Mol. Microbiol. 61:33-45(2006).
RN   [12]
RP   INHIBITION OF FTSZ GTPASE ACTIVITY, INTERACTION WITH FTSZ, AND SUBUNIT.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=17428494; DOI=10.1016/j.jmb.2007.03.025;
RA   Small E., Marrington R., Rodger A., Scott D.J., Sloan K., Roper D.,
RA   Dafforn T.R., Addinall S.G.;
RT   "FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE,
RT   involves a conformational change in bound GTP.";
RL   J. Mol. Biol. 369:210-221(2007).
RN   [13]
RP   CRYSTALLIZATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=16511026; DOI=10.1107/s1744309105003945;
RA   Addinall S.G., Johnson K.A., Dafforn T., Smith C., Rodger A., Gomez R.P.,
RA   Sloan K., Blewett A., Scott D.J., Roper D.I.;
RT   "Expression, purification and crystallization of the cell-division protein
RT   YgfE from Escherichia coli.";
RL   Acta Crystallogr. F 61:305-307(2005).
CC   -!- FUNCTION: Activator of cell division through the inhibition of FtsZ
CC       GTPase activity, therefore promoting FtsZ assembly into bundles of
CC       protofilaments necessary for the formation of the division Z ring. It
CC       is recruited early at mid-cell but it is not essential for cell
CC       division. {ECO:0000269|PubMed:15060045}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000269|PubMed:15317782,
CC       ECO:0000269|PubMed:17428494}.
CC   -!- INTERACTION:
CC       P0ADS2; P0AF36: zapB; NbExp=4; IntAct=EBI-1119901, EBI-1134093;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12368265}.
CC       Note=Localizes at mid-cell.
CC   -!- SIMILARITY: Belongs to the ZapA family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U28377; AAA69078.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75948.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76975.1; -; Genomic_DNA.
DR   EMBL; D90281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M12965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; F65075; F65075.
DR   RefSeq; NP_417386.1; NC_000913.3.
DR   RefSeq; WP_001276008.1; NZ_STEB01000001.1.
DR   PDB; 4P1M; X-ray; 1.95 A; A/B=1-109.
DR   PDBsum; 4P1M; -.
DR   AlphaFoldDB; P0ADS2; -.
DR   SMR; P0ADS2; -.
DR   BioGRID; 4262169; 355.
DR   IntAct; P0ADS2; 8.
DR   STRING; 511145.b2910; -.
DR   jPOST; P0ADS2; -.
DR   PaxDb; 511145-b2910; -.
DR   EnsemblBacteria; AAC75948; AAC75948; b2910.
DR   GeneID; 75205253; -.
DR   GeneID; 947404; -.
DR   KEGG; ecj:JW2878; -.
DR   KEGG; eco:b2910; -.
DR   PATRIC; fig|1411691.4.peg.3822; -.
DR   EchoBASE; EB2716; -.
DR   eggNOG; COG3027; Bacteria.
DR   HOGENOM; CLU_116623_3_0_6; -.
DR   InParanoid; P0ADS2; -.
DR   OMA; NICYELH; -.
DR   OrthoDB; 5917174at2; -.
DR   PhylomeDB; P0ADS2; -.
DR   BioCyc; EcoCyc:EG12878-MONOMER; -.
DR   PRO; PR:P0ADS2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR   GO; GO:0030428; C:cell septum; IMP:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0051301; P:cell division; IMP:EcoCyc.
DR   GO; GO:0000917; P:division septum assembly; IMP:EcoliWiki.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR   GO; GO:0000921; P:septin ring assembly; IDA:EcoliWiki.
DR   Gene3D; 1.20.5.50; -; 1.
DR   Gene3D; 3.30.160.880; Cell division protein ZapA protomer, N-terminal domain; 1.
DR   HAMAP; MF_02012; ZapA_type1; 1.
DR   InterPro; IPR007838; Cell_div_ZapA-like.
DR   InterPro; IPR036192; Cell_div_ZapA-like_sf.
DR   InterPro; IPR023771; Cell_div_ZapA_eubact.
DR   InterPro; IPR042233; Cell_div_ZapA_N.
DR   PANTHER; PTHR34981; CELL DIVISION PROTEIN ZAPA; 1.
DR   PANTHER; PTHR34981:SF1; CELL DIVISION PROTEIN ZAPA; 1.
DR   Pfam; PF05164; ZapA; 1.
DR   SUPFAM; SSF102829; Cell division protein ZapA-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Reference proteome; Septation.
FT   CHAIN           1..109
FT                   /note="Cell division protein ZapA"
FT                   /id="PRO_0000169350"
FT   COILED          21..99
FT                   /evidence="ECO:0000255"
FT   CONFLICT        14
FT                   /note="S -> Y (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:4P1M"
FT   STRAND          13..18
FT                   /evidence="ECO:0007829|PDB:4P1M"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:4P1M"
FT   HELIX           24..45
FT                   /evidence="ECO:0007829|PDB:4P1M"
FT   HELIX           50..101
FT                   /evidence="ECO:0007829|PDB:4P1M"
SQ   SEQUENCE   109 AA;  12594 MW;  26777CC2B2B71148 CRC64;
     MSAQPVDIQI FGRSLRVNCP PDQRDALNQA ADDLNQRLQD LKERTRVTNT EQLVFIAALN
     ISYELAQEKA KTRDYAASME QRIRMLQQTI EQALLEQGRI TEKTNQNFE
//

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