ID U1ZK74_9PSED Unreviewed; 364 AA.
AC U1ZK74;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=N878_03205 {ECO:0000313|EMBL:ERI53854.1};
OS Pseudomonas sp. EGD-AK9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI53854.1, ECO:0000313|Proteomes:UP000016488};
RN [1] {ECO:0000313|EMBL:ERI53854.1, ECO:0000313|Proteomes:UP000016488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA Purohit H.J.;
RT "Indian agricultural soil isolates capable of pesticide degradation.";
RL Submitted (AUG-2013) 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:ERI53854.1}.
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; AVOF01000063; ERI53854.1; -; Genomic_DNA.
DR RefSeq; WP_021442299.1; NZ_AVOF01000063.1.
DR AlphaFoldDB; U1ZK74; -.
DR PATRIC; fig|1386078.3.peg.665; -.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000016488; 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 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 364 AA; 41959 MW; 9493451DB016B063 CRC64;
MTPFERYQAD LQRPDFFHDA AQENAVRHLQ RLYDELVAAD QGKGGLLGKL FGKKPQGPVK
GIYFWGGVGR GKTYLVDTFF DALPFERKMR THFHRFMKRV HEEMRTLKGE KNPLTIIGRR
FADEARVICF DEFFVSDITD AMILATLLEE LFKNGVSLVA TSNIVPDGLY KDGLQRARFL
PAIALLKQHT DIVNVDSGVD YRLRALEQAE LFHFPLDAEA EVSLDKSFRS LLPEHCSVQE
HEALMIENRP IVARKVGDDV AWFEFRELCD GPRSQNDYIE LGKIFHAVIL ANVEQMSTAK
DDMARRFINL VDEFYDRNVK LIISAEVELK DLYTGGRLTF EFQRTLSRLL EMQSHEFLSR
PHKP
//
