ID D0Z1W7_PHODD Unreviewed; 367 AA.
AC D0Z1W7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=VDA_003531 {ECO:0000313|EMBL:EEZ42498.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ42498.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ42498.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ42498.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) 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 ---------------------------------------------------------------------------
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; ADBS01000001; EEZ42498.1; -; Genomic_DNA.
DR RefSeq; WP_005303712.1; NZ_ADBS01000001.1.
DR AlphaFoldDB; D0Z1W7; -.
DR eggNOG; COG1485; Bacteria.
DR Proteomes; UP000003579; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003579}.
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; 42894 MW; B4E9F23BC89653E7 CRC64;
MTPIEKYQLD LKQPDFVADP YQAAVIEQFD ELYQNLLQQK PEQAKVSFWH QWFPPSQQAK
SVPIKGLYLW GGVGRGKTYL MDLFFETLPT QRKQRIHFHR FMQYVHRQLG QLEQQVDPLK
EVAKTLNKQI DVLCFDEFFV SDITDAMILA NLFEALFAQG IILVATSNIP PHDLYRNGLQ
RARFLPTIAL LEQHCKVIHL DSPTDYRLRQ LEQAKLFYYP LTDVVAEQLQ QAFISLSREP
RIYGQPIHIN NRAIATLGQA SDVLYCQFSA LCQTARSAND YIEIARLYHT VIVEGIPMMD
DGQNDAMRRF IALVDEFYER RVKLLISSQI SIEHMYQGTL LRFEFERCCS RLIEMQSHDY
LAQQHRP
//
