ID A0A2T5MIK9_9GAMM Unreviewed; 365 AA.
AC A0A2T5MIK9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CJD38_07175 {ECO:0000313|EMBL:PTU32423.1};
OS Stenotrophobium rhamnosiphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stenotrophobium.
OX NCBI_TaxID=2029166 {ECO:0000313|EMBL:PTU32423.1, ECO:0000313|Proteomes:UP000244248};
RN [1] {ECO:0000313|EMBL:PTU32423.1, ECO:0000313|Proteomes:UP000244248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GT1R17 {ECO:0000313|EMBL:PTU32423.1,
RC ECO:0000313|Proteomes:UP000244248};
RA Liu Q., Xin Y.-H.;
RT "Novel species isolated from glacier.";
RL Submitted (APR-2018) 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:PTU32423.1}.
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DR EMBL; QANS01000002; PTU32423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5MIK9; -.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000244248; 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 ECO:0000313|EMBL:PTU32423.1}; 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:UP000244248}.
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 365 AA; 41574 MW; F85958E2B2A6E429 CRC64;
MATPQELLSP IQRYQRDLAG DNFQRDESQA QAVDALQRVY EALLAAPPKK RFGSSRLRWP
AVAGLYMWGG VGRGKTYLMD TFYDALPFDR KMRTHFHRFM LEVHQRRQHY AHETDPIGKV
ALEFAAKIRV LCFDEFYVSD IADAMILGRL TEVLFENGVT LIATSNVVPD NLYKDGLQRA
NFLPAIDRLK KSVKVLNVDG GIDHRLRALT RAEVYHSPCD ATSEQNMLRD FSAIAGCTGV
ENVEMPIHDR IIVARRLADG VAWFDFAAVC DGPRSAADYI EIGRTHHTVL LSHVPQLTVF
TEDAARRFIN LVDEFYDRGV KLIITADVPQ EKLYAGLKLR FEFQRTLSRL QEMQSQEYLA
KPHLS
//
