ZAPE_ECOLI
ID ZAPE_ECOLI Reviewed; 375 AA.
AC P64612; P46442; Q2M8Y1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=b3232, JW3201;
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 FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, GENE NAME, AND MUTAGENESIS OF LYS-84.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24595368; DOI=10.1128/mbio.00022-14;
RA Marteyn B.S., Karimova G., Fenton A.K., Gazi A.D., West N., Touqui L.,
RA Prevost M.C., Betton J.M., Poyraz O., Ladant D., Gerdes K.,
RA Sansonetti P.J., Tang C.M.;
RT "ZapE is a novel cell division protein interacting with FtsZ and modulating
RT the Z-ring dynamics.";
RL MBio 5:E22-E22(2014).
CC -!- FUNCTION: Reduces the stability of FtsZ polymers in the presence of
CC ATP. Required for cell division under low-oxygen conditions. Hydrolyzes
CC ATP but not GTP. {ECO:0000255|HAMAP-Rule:MF_01919,
CC ECO:0000269|PubMed:24595368}.
CC -!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01919,
CC ECO:0000269|PubMed:24595368}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01919,
CC ECO:0000269|PubMed:24595368}. Note=Localizes to the constricting Z-ring
CC during late stages of the cell division process.
CC -!- DISRUPTION PHENOTYPE: Mutants have no growth defect in aerobic
CC conditions. However, inactivation leads to a stress-dependent elongated
CC phenotype (in anaerobiosis or at temperatures over 37 degrees Celsius).
CC {ECO:0000269|PubMed:24595368}.
CC -!- MISCELLANEOUS: ZapE abundance has to be tightly regulated to allow cell
CC division. Loss or overexpression of ZapE alters Z-ring stability and
CC leads to bacterial filamentation (PubMed:24595368).
CC {ECO:0000305|PubMed:24595368}.
CC -!- SIMILARITY: Belongs to the AFG1 ATPase family. ZapE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01919}.
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DR EMBL; U18997; AAA58034.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76264.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77275.1; -; Genomic_DNA.
DR PIR; B65115; B65115.
DR RefSeq; NP_417699.1; NC_000913.3.
DR RefSeq; WP_001192332.1; NZ_SSZK01000034.1.
DR AlphaFoldDB; P64612; -.
DR SMR; P64612; -.
DR BioGRID; 4261913; 23.
DR DIP; DIP-48198N; -.
DR IntAct; P64612; 1.
DR STRING; 511145.b3232; -.
DR jPOST; P64612; -.
DR PaxDb; P64612; -.
DR PRIDE; P64612; -.
DR EnsemblBacteria; AAC76264; AAC76264; b3232.
DR EnsemblBacteria; BAE77275; BAE77275; BAE77275.
DR GeneID; 947821; -.
DR KEGG; ecj:JW3201; -.
DR KEGG; eco:b3232; -.
DR PATRIC; fig|511145.12.peg.3329; -.
DR EchoBASE; EB2670; -.
DR eggNOG; COG1485; Bacteria.
DR HOGENOM; CLU_008681_0_4_6; -.
DR InParanoid; P64612; -.
DR OMA; QKREYWE; -.
DR PhylomeDB; P64612; -.
DR BioCyc; EcoCyc:G7680-MON; -.
DR PRO; PR:P64612; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000169487"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 84
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:24595368"
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
