ID A0A0S4I6C2_9PSED Unreviewed; 364 AA.
AC A0A0S4I6C2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=PYEL_10090 {ECO:0000313|EMBL:CRN05252.1};
OS Pseudomonas sp. URMO17WK12:I11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1283291 {ECO:0000313|EMBL:CRN05252.1, ECO:0000313|Proteomes:UP000062067};
RN [1] {ECO:0000313|Proteomes:UP000062067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Falquet L., Falquet L.;
RL Submitted (JUN-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; LN865164; CRN05252.1; -; Genomic_DNA.
DR RefSeq; WP_027914467.1; NZ_VEIM01000008.1.
DR AlphaFoldDB; A0A0S4I6C2; -.
DR GeneID; 64093394; -.
DR PATRIC; fig|1283291.5.peg.983; -.
DR Proteomes; UP000062067; Chromosome 1.
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; 41952 MW; 197375A1268FCA70 CRC64;
MTPLERYQAD LKRPDFFHDA AQETAVRHLQ RLYDDLVQAQ NNKPGVFGKL FGKKEQTPVK
GLYFWGGVGR GKTYLVDTFF EALPFKQKMR THFHRFMKRV HEEMKTLKGE KNPLTIIAKR
FSDEAKVICF DEFFVSDITD AMILGTLMEE LFKNGVSLVA TSNIVPDGLY KDGLQRARFL
PAIAMIKQYT DVVNVDSGVD YRLRHLEQAE LFHYPLDEAA QQSMRASFKA LTPECTAAVE
NDVLMIENRP IHALRTCDDV AWFDFRALCD GPRSQNDYIE LGKIFHAVLL SNVEQMGVAS
DDIARRFINM VDEFYDRNVK LIISAEVELK DLYTGGRLSF EFQRTLSRLL EMQSHEFLSR
AHKP
//
