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   03-AUG-2022, entry version 122.
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; Proteobacteria; 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; P0ADS2; -.
DR   PRIDE; P0ADS2; -.
DR   EnsemblBacteria; AAC75948; AAC75948; b2910.
DR   EnsemblBacteria; BAE76975; BAE76975; BAE76975.
DR   GeneID; 67415204; -.
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   PhylomeDB; P0ADS2; -.
DR   BioCyc; EcoCyc:EG12878-MON; -.
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:EcoliWiki.
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; 3.30.160.880; -; 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; PTHR34981; 1.
DR   Pfam; PF05164; ZapA; 1.
DR   SUPFAM; SSF102829; SSF102829; 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