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Database: UniProt
Entry: A0A0F5ZXM3_9GAMM
LinkDB: A0A0F5ZXM3_9GAMM
Original site: A0A0F5ZXM3_9GAMM 
ID   A0A0F5ZXM3_9GAMM        Unreviewed;       367 AA.
AC   A0A0F5ZXM3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ORFNames=RN22_13065 {ECO:0000313|EMBL:KKD60062.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD60062.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD60062.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD60062.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reduces the stability of FtsZ polymers in the presence of
CC       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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKD60062.1}.
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DR   EMBL; LASY01000055; KKD60062.1; -; Genomic_DNA.
DR   RefSeq; WP_046304897.1; NZ_LASY01000055.1.
DR   AlphaFoldDB; A0A0F5ZXM3; -.
DR   PATRIC; fig|1581149.3.peg.3421; -.
DR   OrthoDB; 9774491at2; -.
DR   Proteomes; UP000033732; Unassembled WGS sequence.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01919; ZapE; 1.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR030870; ZapE.
DR   NCBIfam; NF040713; ZapE; 1.
DR   PANTHER; PTHR12169:SF6; AFG1-LIKE ATPASE; 1.
DR   PANTHER; PTHR12169; ATPASE N2B; 1.
DR   Pfam; PF03969; AFG1_ATPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01919}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01919};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01919}.
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ   SEQUENCE   367 AA;  42623 MW;  1BD9CD6F3A634CB7 CRC64;
     MTPLEQYHND LQRPDFFEDA SQRNAVEKLE DLYHRLIKRA HAPVEKQGFL ESLFKKKTPV
     KAPEKGLYFW GGVGRGKTYL VDTFFESLPF DKKLRMHFHR FMHRVHHELK LLDGEQDPLQ
     KIADKLADEA HILCFDEFFV SDITDAMILG TLMEALFERG ICLVATSNIV PDELYRNGLQ
     RARFLPAIAL INQHCEVVNV DAGTDYRLRT LEQAEIFHFP LDEAAGENLK EYFYKLATEP
     CHESLEIEIN NRKLIAEREA EGVVHFEFAT LCDSPRSQSD YIEIARLYHT VLLANVPQMG
     LSKDDAARRF IAMVDEFYER HVKLIISAEV ALNSLYTDGR LSFEFRRCIS RLKEMQSHDY
     LALEHLP
//
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