ID A0A086D3L7_9GAMM Unreviewed; 393 AA.
AC A0A086D3L7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=GY26_10760 {ECO:0000313|EMBL:KFF49031.1};
OS Gammaproteobacteria bacterium MFB021.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1492922 {ECO:0000313|EMBL:KFF49031.1, ECO:0000313|Proteomes:UP000028732};
RN [1] {ECO:0000313|EMBL:KFF49031.1, ECO:0000313|Proteomes:UP000028732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB021 {ECO:0000313|EMBL:KFF49031.1,
RC ECO:0000313|Proteomes:UP000028732};
RA Joseph T.C., Baby A., Varghese A.M., Reghunathan D., Murugadas V.,
RA Lalitha K.V.;
RT "Draft Genome sequence of a halophilic and highly halotolerant unknown
RT Gammaproteobacteria strain MFB021.";
RL Submitted (JUN-2014) 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:KFF49031.1}.
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DR EMBL; JNVT01000074; KFF49031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086D3L7; -.
DR STRING; 1492922.GY26_10760; -.
DR eggNOG; COG1485; Bacteria.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000028732; 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 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 393 AA; 44248 MW; 7CEC8C66345DA50E CRC64;
MTASRSATSA ANAQTPIARY RADLERDDFS YDAAQENAVK HLQRLYDDLL RAPAPKPSVT
GGGDSALSKV AGLFGKRKAA APEAPAKPAV MGLYFWGGVG RGKTYLVDVF FEALPFERKM
RTHFNRFMQR VHRELEAHKG EKNPLTQIAA QFAREARVIC FDEFYVKDIT DAMILGNLME
ALFAQGVVLV ATSNIVPDDL YKDGLQRSRF LPAIDLLKRN CEVVNVDSGV DYRLRALEQV
EIFHSPLDAE AERSLARSFR SVAGSEGREN AKLTINHREL SARRLCEGVV WFDFKMICDG
PRSQNDYIEL SREYHTVLVS NVPRMGAGSD DQARRFISMV DEFYDRAVKL LLSAETEVES
LYTGGNLSFE FERTLSRLQE MQSREYLALA HKP
//
