ID A0A0S2KF89_9GAMM Unreviewed; 405 AA.
AC A0A0S2KF89;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=PS2015_2319 {ECO:0000313|EMBL:ALO46954.1};
OS Pseudohongiella spirulinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO46954.1, ECO:0000313|Proteomes:UP000065641};
RN [1] {ECO:0000313|EMBL:ALO46954.1, ECO:0000313|Proteomes:UP000065641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO46954.1,
RC ECO:0000313|Proteomes:UP000065641};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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; CP013189; ALO46954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2KF89; -.
DR STRING; 1249552.PS2015_2319; -.
DR KEGG; pspi:PS2015_2319; -.
DR PATRIC; fig|1249552.3.peg.2332; -.
DR Proteomes; UP000065641; 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:UP000065641}.
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 405 AA; 45815 MW; E36981712907CC8A CRC64;
MLFEADLLLG FVVRHGLECA SFHVERKIQG FSTMQMASPR QRYQADLDAG KLTPDPAQRA
AIEKVQQLYE ALLNQSNRHS RLSLNPLRWL RVQAASSAAP QGIYFYGGVG RGKTYIMDLF
YESLPFTQKQ RTHFHRFMQQ VHAALAALKN QKNPLELVAG QIAGSARVLC FDEFFVSDIG
DAMILGGLLE HLMARNVVLV ATSNIHPDGL YANGLQRARF LPAIELLKKH TQIVELDGGV
DYRLRTLQQA CLYFHPLGAD AEAGLLQAME RLSSGHAEIS ENVEIEVLGR AIKVRRVCDE
IAWFDCRQLC DGARSAFDYI ELARLYHTII LSDVPQMDGD MDNIARRFVS LVDELYDRHV
KLIISAAVPL TQLYSGHDLA FVFERTRSRL LEMQSEEYLA REHRP
//
