ID A0A1B2R030_9BORD Unreviewed; 496 AA.
AC A0A1B2R030;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN ORFNames=AKI39_06065 {ECO:0000313|EMBL:AOB30353.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB30353.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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 -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC {ECO:0000256|ARBA:ARBA00007125}.
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DR EMBL; CP012334; AOB30353.1; -; Genomic_DNA.
DR RefSeq; WP_066633678.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2R030; -.
DR STRING; 1697043.AKI39_06065; -.
DR KEGG; boh:AKI39_06065; -.
DR PATRIC; fig|1697043.4.peg.1250; -.
DR OrthoDB; 9793035at2; -.
DR Proteomes; UP000093512; Chromosome.
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:SF0; RETROGRADE REGULATION PROTEIN 2; 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 Reference proteome {ECO:0000313|Proteomes:UP000093512}.
FT DOMAIN 22..304
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 312..480
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 496 AA; 55286 MW; CECD0C1262E0FDF8 CRC64;
MDHLLAAVDL GSNSFRLSIG RVVQQEGAAQ IYQIDRLKET VRLAAGLDAD KHLSRDAVDR
AIEVLERFGE RLRNFHPSRV RAVATNTFRV ARNTAEFLPR AGAALGFPIE VIAGREEARL
IFSGVVHTLP PSQNKRLVID IGGGSTEVII GKGYEPALMS SLYMGCVSYS RQFFRDGVVD
AHQMKLAELA ARREAEVIAK QYRKMGWKEA YGSSGTAKAL YAILTECGFS NRGITRAGLA
KLKDRIIRSG RVIPSELPGI KVERADVLPG GLAIMSALFD ELNIDVMHTG DGALRLGVLY
DLLGRDDQHD KRDESVRQFM KRYHIDVNQA ARVRRAALTL FKESGIEAGT ERHELAHALG
WAADLHEIGL SIAHNDYHKH SAYVLGNADM PGFSRDDQRL LALLALGHHG KLGKLEPLVR
NREEWLAILC LRLAVLLFRR REDLAALPLS VSVRGDSIVV RVRHDWLAEH PLSDFTLRAE
ESEWRKVGFS FELLEF
//
