ID A3QI63_SHELP Unreviewed; 368 AA.
AC A3QI63;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=Shew_3295 {ECO:0000313|EMBL:ABO25161.1};
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO25161.1, ECO:0000313|Proteomes:UP000001558};
RN [1] {ECO:0000313|EMBL:ABO25161.1, ECO:0000313|Proteomes:UP000001558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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; CP000606; ABO25161.1; -; Genomic_DNA.
DR RefSeq; WP_011867091.1; NC_009092.1.
DR AlphaFoldDB; A3QI63; -.
DR STRING; 323850.Shew_3295; -.
DR KEGG; slo:Shew_3295; -.
DR eggNOG; COG1485; Bacteria.
DR HOGENOM; CLU_008681_0_4_6; -.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000001558; 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:UP000001558}.
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 368 AA; 42191 MW; D6891F0E54ED3F16 CRC64;
MSHLTPWQHY QADLQRDDFS YDPAQEQAVK ALQRVYDELL AAQQKPSGMA KLLGFLAKPA
PQVQGLYLWG GVGRGKTYLM DTFYDALPGE RKLRAHFHRF MHQIHLDLDG LKGQRDPLLV
IAKRMAERYQ VICFDEFFVS DITDAMLLGT LFQALFAEGV ALVATSNIIP DELYRNGLQR
ARFLPAIALI NKHCQVLNVD SGIDYRLRTL EQAEIYHYPL DPQADKNLLS YFQQLAPESE
VSREAIDIDG REIGIRQQAQ GVLLIDFRDL CDGPRSQRDY MELACLYHTV LLSGVEQMGS
QSTGDDIARR FLAMVDEFYE RHVKLIISAE VALEEIYTQG LLSFEFRRCR SRLTEMQSHD
YLALEHLP
//
