ID   ZAPE_ECO57              Reviewed;         375 AA.
AC   P64613; P46442;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cell division protein ZapE {ECO:0000255|HAMAP-Rule:MF_01919};
DE   AltName: Full=Z ring-associated protein ZapE {ECO:0000255|HAMAP-Rule:MF_01919};
GN   Name=zapE {ECO:0000255|HAMAP-Rule:MF_01919}; Synonyms=yhcM;
GN   OrderedLocusNames=Z4591, ECs4105;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Reduces the stability of FtsZ polymers in the presence of
CC       ATP. {ECO:0000255|HAMAP-Rule:MF_01919}.
CC   -!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01919}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01919}.
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family. ZapE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01919}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005174; AAG58360.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37528.1; -; Genomic_DNA.
DR   PIR; A91142; A91142.
DR   PIR; D85987; D85987.
DR   RefSeq; NP_312132.1; NC_002695.1.
DR   RefSeq; WP_001192332.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P64613; -.
DR   SMR; P64613; -.
DR   STRING; 155864.EDL933_4454; -.
DR   EnsemblBacteria; AAG58360; AAG58360; Z4591.
DR   EnsemblBacteria; BAB37528; BAB37528; ECs_4105.
DR   GeneID; 916046; -.
DR   KEGG; ece:Z4591; -.
DR   KEGG; ecs:ECs_4105; -.
DR   PATRIC; fig|386585.9.peg.4286; -.
DR   eggNOG; COG1485; Bacteria.
DR   HOGENOM; CLU_008681_0_4_6; -.
DR   OMA; QKREYWE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01919; ZapE; 1.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR030870; ZapE.
DR   PANTHER; PTHR12169; PTHR12169; 1.
DR   Pfam; PF03969; AFG1_ATPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Cell division protein ZapE"
FT                   /id="PRO_0000169488"
FT   BINDING         78..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01919"
SQ   SEQUENCE   375 AA;  43064 MW;  24866D51E551452D CRC64;
     MQSVTPTSQY LKALNEGSHQ PDDVQKEAVS RLEIIYQELI NSTPPAPRTS GLMARVGKLW
     GKREDTKHTP VRGLYMWGGV GRGKTWLMDL FYQSLPGERK QRLHFHRFML RVHEELTALQ
     GQTDPLEIIA DRFKAETDVL CFDEFFVSDI TDAMLLGGLM KALFARGITL VATSNIPPDE
     LYRNGLQRAR FLPAIDAIKQ HCDVMNVDAG VDYRLRTLTQ AHLWLSPLHD ETRAQMDKLW
     LALAGGKREN SPTLEINHRP LATMGVENQT LAVSFTTLCV DARSQHDYIA LSRLFHTVML
     FDVPVMTRLM ESEARRFIAL VDEFYERHVK LVVSAEVPLY EIYQGDRLKF EFQRCLSRLQ
     EMQSEEYLKR EHLAG