ID A0A0F6TRT7_9GAMM Unreviewed; 362 AA.
AC A0A0F6TRT7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=TQ33_1728 {ECO:0000313|EMBL:AKE52669.1};
OS Kangiella geojedonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE52669.1, ECO:0000313|Proteomes:UP000034071};
RN [1] {ECO:0000313|EMBL:AKE52669.1, ECO:0000313|Proteomes:UP000034071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCS-5 {ECO:0000313|EMBL:AKE52669.1,
RC ECO:0000313|Proteomes:UP000034071};
RA Kim K.M.;
RT "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL Submitted (FEB-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}.
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DR EMBL; CP010975; AKE52669.1; -; Genomic_DNA.
DR RefSeq; WP_046561713.1; NZ_CP010975.1.
DR AlphaFoldDB; A0A0F6TRT7; -.
DR STRING; 914150.TQ33_1728; -.
DR KEGG; kge:TQ33_1728; -.
DR PATRIC; fig|914150.5.peg.1751; -.
DR HOGENOM; CLU_008681_0_4_6; -.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000034071; Chromosome.
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:UP000034071}.
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 362 AA; 41675 MW; D06926D5B2E328C7 CRC64;
MTPLEKYQQD LANGFSKDPA QEEAVKALQT VYDDLMASRP TSGFMQKLTR WLSGDSQPVK
GLYMWGGVGR GKTYLMDTFF SVLPLKAKIR LHFHRFMHEV HNELKALAGE KNPLVKIADQ
LAERAKIICF DEFFVTDITD AMILGSLFEE LFKRHVVLVA TSNIPPDRLY WNGLQRERFL
PAIKLIQENC EVLNVDAGID YRMRTLEKAE IYHYPLDKAA NANMREYFKQ LAATEGQDNC
KLKVDGRLID TVKLSDSVVW FTFKAICQTE RSASDYIEIS RGYHTVFVGQ VPQMDDSLND
AVRRFIALID EFYERHVKLI ISAEVPMEEL YTGKGLAFEF KRTLSRLQEM QSKDYLSLEH
LA
//
