ID A0A317P7B5_9GAMM Unreviewed; 419 AA.
AC A0A317P7B5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=DER72_101193 {ECO:0000313|EMBL:PWV83012.1};
OS Halomonas sp. A11-A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2183985 {ECO:0000313|EMBL:PWV83012.1, ECO:0000313|Proteomes:UP000246506};
RN [1] {ECO:0000313|EMBL:PWV83012.1, ECO:0000313|Proteomes:UP000246506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A11-A {ECO:0000313|EMBL:PWV83012.1,
RC ECO:0000313|Proteomes:UP000246506};
RA Wrighton K.;
RT "Subsurface microbial communities from deep shales in Ohio and West
RT Virginia, USA.";
RL Submitted (MAY-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:PWV83012.1}.
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DR EMBL; QGTM01000001; PWV83012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317P7B5; -.
DR Proteomes; UP000246506; 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:PWV83012.1}; 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 REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01919"
SQ SEQUENCE 419 AA; 48207 MW; 22E712FE99F5BE8E CRC64;
MAVRASASMR IMRNHLQPRW SEPRMSATPT PPESRDARLS PTERYRADLK RDDFQYDPAQ
EQAVAHLQRL HDDLMAAPRR RPRAVPPQGK IASRMAGLFG KRSRQASAPE SVLPEVTGLY
FWGGVGRGKT YLVDAFYESL PFPEKMRTHF HRFMQRVHNE LTHYKGEKNP LKLIAAKFAS
EARVICFDEF FVKDITDAMI LANLLEALFE HGVVLVATSN IVPDDLYKDG LQRARFLPAI
ELLKRHCEVV NVDSGIDYRL RALERAEIFH APLDAAAESE LARSFREIAG HEGEADAPIE
INHRVLRARR LHDDVVWFEF RELCDGPRSQ NDYIELAREF HTVLVANVTR MSGATDDQAR
RFINMVDEFY DRGVKLLMSA EVPAERLYAD GRLEFEFQRT LSRLQEMQSH EYLALPHKP
//
