ID A0A0P7ZA56_9GAMM Unreviewed; 392 AA.
AC A0A0P7ZA56;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=HLUCCA13_03945 {ECO:0000313|EMBL:KPQ25680.1};
OS Halomonas sp. HL-48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1479235 {ECO:0000313|EMBL:KPQ25680.1, ECO:0000313|Proteomes:UP000050569};
RN [1] {ECO:0000313|EMBL:KPQ25680.1, ECO:0000313|Proteomes:UP000050569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-48 {ECO:0000313|EMBL:KPQ25680.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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}.
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:KPQ25680.1}.
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DR EMBL; LJZS01000003; KPQ25680.1; -; Genomic_DNA.
DR RefSeq; WP_027335394.1; NZ_LJZS01000003.1.
DR AlphaFoldDB; A0A0P7ZA56; -.
DR STRING; 1479235.GCA_000686925_00326; -.
DR PATRIC; fig|1479235.4.peg.1758; -.
DR eggNOG; COG1485; Bacteria.
DR OrthoDB; 9774491at2; -.
DR Proteomes; UP000050569; 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}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 392 AA; 44242 MW; 0E665F46A0C62C3D CRC64;
MRATSAGGEP APKAATPMGR YREDLKREGF EYDAAQEAAV AHLQRLYDAL LSTPTTVPKT
VLANKGLKAR MAGLMGKKSS PAEPVTPSVQ GLYFWGGVGR GKTYLVDTFY EALPFADKMR
THFHRFMQRV HNELTHYKGE KNPLTLVASK FASEARVICF DEFFVKDITD AMILANLLEA
LFERGVVLVA TSNIVPDDLY KDGLQRARFV PAIDLLNRHC RVVNVDSGVD YRLRALERAE
IFHSPLDEAA EEELARSFRE IAGHAGEANA PLEINQRVLT TRRLHDDIAW FEFVELCDGP
RSQNDYIELA REFHTIIVSN VPAMRGGDDD QARRFINMVD EFYDRGVKVL MSAEAPVESL
YGDGKLTFEY QRTLSRLQEM QSHEYLALPH KP
//
