ID A0A090TZR9_9VIBR Unreviewed; 367 AA.
AC A0A090TZR9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-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=JCM19240_1781 {ECO:0000313|EMBL:GAL36337.1};
OS Vibrio maritimus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL36337.1, ECO:0000313|Proteomes:UP000029224};
RN [1] {ECO:0000313|EMBL:GAL36337.1, ECO:0000313|Proteomes:UP000029224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL36337.1,
RC ECO:0000313|Proteomes:UP000029224};
RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAL36337.1, ECO:0000313|Proteomes:UP000029224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL36337.1,
RC ECO:0000313|Proteomes:UP000029224};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (SEP-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:GAL36337.1}.
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DR EMBL; BBMT01000010; GAL36337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090TZR9; -.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000029224; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029224}.
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 367 AA; 42556 MW; 048A1A291844BC95 CRC64;
MTPIERYEHD IETNGFQADP AQRTAVEALD KLHDQFSDYL KFEAPPLSMM QKLLGKKPEQ
AVPPKGLYFW GGVGRGKTYL MDAFFDSLPT SRKMRVHFHR FMYRVHDELK RLGDVENPLE
KVADIFESEA KIICFDEFFV SDITDAMILA TLLQELFKRG VVLVATSNIP PENLYRNGLQ
RARFMPAISL IQSQCVVLNV DSGIDYRLRT LEQAEIYHFP LDEAANQNLE RYFNQLVMDD
RVHEASIEIN HRDIDVFAAA DDVLFASFAQ LCQTMRSQND YIEMSRIYHT VLLADVKQMD
AKLDDAARRF IALVDEFYER RVKLIISAEV ALEELYTQGQ LEFEFKRCIS RLTEMQSHDY
LASEHLP
//
