(data stored in SCRATCH zone)

SWISSPROT: C5B746_EDWI9

ID   C5B746_EDWI9            Unreviewed;       377 AA.
AC   C5B746;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 41.
DE   RecName: Full=Cell division protein ZapE {ECO:0000256|HAMAP-Rule:MF_01919};
DE   AltName: Full=Z ring-associated protein ZapE {ECO:0000256|HAMAP-Rule:MF_01919};
GN   Name=zapE {ECO:0000256|HAMAP-Rule:MF_01919};
GN   OrderedLocusNames=NT01EI_0591 {ECO:0000313|EMBL:ACR67820.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67820.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reduces the stability of FtsZ polymers in the presence
CC       of ATP. {ECO:0000256|HAMAP-Rule:MF_01919}.
CC   -!- SUBUNIT: Interacts with FtsZ. {ECO:0000256|HAMAP-Rule:MF_01919}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01919}.
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family. ZapE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01919}.
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DR   EMBL; CP001600; ACR67820.1; -; Genomic_DNA.
DR   RefSeq; WP_015870018.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0591; -.
DR   EnsemblBacteria; ACR67820; ACR67820; NT01EI_0591.
DR   GeneID; 7960359; -.
DR   KEGG; eic:NT01EI_0591; -.
DR   PATRIC; fig|634503.3.peg.536; -.
DR   eggNOG; ENOG4105D6Z; Bacteria.
DR   eggNOG; COG1485; LUCA.
DR   HOGENOM; HOG000259599; -.
DR   KO; K06916; -.
DR   OMA; FYDRNVK; -.
DR   OrthoDB; POG091H05QG; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-HAMAP.
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;
DR   PRODOM; C5B746.
DR   SWISS-2DPAGE; C5B746.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   NP_BIND      81     88       ATP. {ECO:0000256|HAMAP-Rule:MF_01919}.
SQ   SEQUENCE   377 AA;  42467 MW;  44CEFDAD2175ED62 CRC64;
     MFSPYALTHD TPLARYRAAL AVGDYQPDAA QQRAVEALDE IHRQWTMRWQ AAAPAGWRTR
     LPHWLGGRRI AEPITGLYLW GGVGRGKTWL MDLFFDTLPG QRKQRLHFHR FMLWVHESLA
     AKQGLADPLA LLADTLKAQA DVLCFDEFFV TDIGDAMLLG TLLPVLLARG VTLVTTSNIP
     PAQLYPNGLQ RGRFLPAIAN IQTYCQVLNV DGGIDYRLRT LTRAHLYLTP LGARTEQAMD
     ALFLRLAGQA GQAGGTLEIN HRQLPVLRRA EAVVALHFSA LCEAPCSSRD YIALAQRYHT
     VLLHGVSAMN SDREECARRF LALVDEFYER RVTLIISASC DMFGLYCGER LTFEYQRCLS
     RLQEMQSEAY LSLPHRP
//

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