ID A0A2K4G5H8_9PSED Unreviewed; 364 AA.
AC A0A2K4G5H8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=C1886_14965 {ECO:0000313|EMBL:POA18857.1};
OS Pseudomonas sp. FW300-N1A1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA18857.1, ECO:0000313|Proteomes:UP000236411};
RN [1] {ECO:0000313|EMBL:POA18857.1, ECO:0000313|Proteomes:UP000236411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA18857.1,
RC ECO:0000313|Proteomes:UP000236411};
RA Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA Alm E.J.;
RT "Whole genome sequencing of deep branching strains shows evolution and
RT exchange across a contaminated watershed.";
RL Submitted (JAN-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:POA18857.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PPSF01000032; POA18857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4G5H8; -.
DR Proteomes; UP000236411; 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:POA18857.1}; 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}.
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; 41911 MW; A5D8AE1293E1A91F CRC64;
MTPLERYQAD LKRPEFFHDA AQETAVRHLQ RLYDDLVAAS QSKPGLLGKL FGKKDQAPVK
GLYFWGGVGR GKTYLVDTFY EALPFKEKSR THFHRFMKRV HEEMKTLGGE KNPLTIIAKR
FSNEARVICF DEFFVSDITD AMILGTLMEE LFKNGVTLVA TSNIVPDGLY KDGLQRARFL
PAIALIKQNT DIVNVDSGVD YRLRHLEQAE LFHFPLDEAS HESLRKSFRA LTPECTAAVE
NDVLMIENRE IRALRTCDDV AWFDFRELCD GPRSQNDYIE LGKIFHAVLL SGVEQMSVTT
DDIARRFINM VDEFYDRNVK LIISAEVELK DLYTGGRLNF EFQRTLSRLL EMQSHEFLSR
AHKP
//
