ID I4ZUA1_9GAMM Unreviewed; 383 AA.
AC I4ZUA1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=HADU_04800 {ECO:0000313|EMBL:EIM39793.1};
OS Acinetobacter sp. HA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM39793.1, ECO:0000313|Proteomes:UP000018434};
RN [1] {ECO:0000313|EMBL:EIM39793.1, ECO:0000313|Proteomes:UP000018434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA {ECO:0000313|EMBL:EIM39793.1,
RC ECO:0000313|Proteomes:UP000018434};
RX PubMed=22933775; DOI=10.1128/JB.01194-12;
RA Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT the Polyphagous Insect Pest Helicoverpa armigera.";
RL J. Bacteriol. 194:5156-5156(2012).
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:EIM39793.1}.
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DR EMBL; AJXD01000017; EIM39793.1; -; Genomic_DNA.
DR RefSeq; WP_004815619.1; NZ_AJXD01000017.1.
DR AlphaFoldDB; I4ZUA1; -.
DR GeneID; 58162865; -.
DR PATRIC; fig|1173062.3.peg.953; -.
DR Proteomes; UP000018434; 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 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 383 AA; 44595 MW; EDCC4DE504F2252A CRC64;
MSDLNSHQHN AFSPLSPAER YAQALSSGQF MPDDAQAIAV HELDRVWVEL IQRFKASKKA
FRRFRRQTSP KGVYMWGGVG RGKTWLMDQF YDSIPFRRKI RMHFHHFMQH VHRELNKLSG
QRNPLDLVAD QIYKDAVVIC FDEFFVSNVT DAMILSDLFQ KLFERGITLV ATSNIAPDGL
YKNGIHRDRF IPTIELVKKN CVILNVDAGV DYRLRVLKQA QLFKFPLTHD NKNWMAQRFS
ALTQTQQHSD EPIIINNRIV ETVAHTEDVL WCEFAELCLK PRSPADFIEI ANIYNTVLVS
NVPHLTDFLN DGTRRFIYLV DEFYDRGVKL LLTSEDNIVD IYQGEKLAFE IERTRSRLLE
MQSDEYLHSE HRQIEKIASS NAE
//
