ID A0A345ZKS7_9GAMM Unreviewed; 509 AA.
AC A0A345ZKS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN Name=ppx {ECO:0000313|EMBL:AXK72352.1};
GN ORFNames=DWG18_08755 {ECO:0000313|EMBL:AXK72352.1};
OS Lysobacter sp. TY2-98.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=2290922 {ECO:0000313|EMBL:AXK72352.1, ECO:0000313|Proteomes:UP000254438};
RN [1] {ECO:0000313|EMBL:AXK72352.1, ECO:0000313|Proteomes:UP000254438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY2-98 {ECO:0000313|EMBL:AXK72352.1,
RC ECO:0000313|Proteomes:UP000254438};
RA Kim S.-G., Park A.-Y., Lee Y.-J.;
RT "Lysobacter sp. nov. isolated from a farm soil.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC ChEBI:CHEBI:43474; EC=3.6.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000209};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC {ECO:0000256|ARBA:ARBA00007125}.
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DR EMBL; CP031413; AXK72352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345ZKS7; -.
DR KEGG; lyt:DWG18_08755; -.
DR OrthoDB; 9793035at2; -.
DR Proteomes; UP000254438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR022371; Exopolyphosphatase.
DR InterPro; IPR048950; Ppx_GppA_C.
DR InterPro; IPR003695; Ppx_GppA_N.
DR InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR NCBIfam; TIGR03706; exo_poly_only; 1.
DR PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR PANTHER; PTHR30005:SF14; EXOPOLYPHOSPHATASE; 1.
DR Pfam; PF02541; Ppx-GppA; 1.
DR Pfam; PF21447; Ppx-GppA_III; 1.
DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:AXK72352.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000254438}.
FT DOMAIN 31..314
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 322..494
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 509 AA; 55441 MW; 780F18DE7216CC3B CRC64;
MNGLLHTARL PLKDGDLLAA VDLGSNSFHM VVASYVLGQL RIVDRIKETI RLAEGLTAAG
ELAAPERERA LECLARFGQR VRDIPPQRVR AIATNTVRRL AVPQSFLAPA ESALGHPIEV
VAGREEARLI YLGVAHEQPP KAGHLRLVID IGGGSTEFII GSGFEAIERE SVQVGSIATT
RRFFGDGKLS RKAWRAGVSA VSAELQQFAG TYRSLGWNEA LGSSGTARAI GEICAAMKLT
KGAITAEALP QVRDRLLQAE RIADINLPGL SSDRQPIIAG GLLVMEAAFE ALGLSRVAVS
KAAMREGILY DMIGRGGLDD PREGSVIALM ERYGIDRAQA QRVEDTAMLL FEQVRDDWSL
DDDDRLMLAR AARLHELGLT IAHSKYHLHG AYVIENSDIA GFSQQQQQFL ASLVRTHRRR
VHKSDFDALP DRLLASARRL AALLRVAVVL HRGHDPAPIP QLDARADGDR LVLTLSADWF
DSRPLLKADV RAEQDYFSGL GIELVIEAA
//