PPX_HAEIN
ID PPX_HAEIN Reviewed; 323 AA.
AC P44828;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative exopolyphosphatase {ECO:0000250|UniProtKB:P0AFL6};
DE Short=ExopolyPase {ECO:0000250|UniProtKB:P0AFL6};
DE EC=3.6.1.11 {ECO:0000250|UniProtKB:P0AFL6};
GN Name=ppx; OrderedLocusNames=HI_0695;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC orthophosphate processively from the ends of the polyP chain.
CC {ECO:0000250|UniProtKB:P0AFL6}.
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:0000250|UniProtKB:P0AFL6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AFL6};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AFL6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AFL6};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P0AFL6}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. Compared with other ppx
CC it lacks 200 residues at the C-terminal region. {ECO:0000305}.
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DR EMBL; L42023; AAC22355.1; -; Genomic_DNA.
DR PIR; C64087; C64087.
DR RefSeq; NP_438855.1; NC_000907.1.
DR RefSeq; WP_005694580.1; NC_000907.1.
DR AlphaFoldDB; P44828; -.
DR SMR; P44828; -.
DR STRING; 71421.HI_0695; -.
DR EnsemblBacteria; AAC22355; AAC22355; HI_0695.
DR KEGG; hin:HI_0695; -.
DR PATRIC; fig|71421.8.peg.727; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_1_1_6; -.
DR OMA; IGCVRMT; -.
DR PhylomeDB; P44828; -.
DR BioCyc; HINF71421:G1GJ1-730-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR022371; Exopolyphosphatase.
DR InterPro; IPR003695; Ppx_GppA.
DR Pfam; PF02541; Ppx-GppA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR03706; exo_poly_only; 1.
PE 5: Uncertain;
KW Cell membrane; Hydrolase; Magnesium; Membrane; Reference proteome.
FT CHAIN 1..323
FT /note="Putative exopolyphosphatase"
FT /id="PRO_0000194302"
SQ SEQUENCE 323 AA; 35566 MW; 5B7E9BBEFE780FB6 CRC64;
MNDSILEPKH RGNVREIAAI DLGSNSFHMI VARIVNGSIQ VLSRLKQKVK LAEGLDENAV
LNQEAITRGV NCLALFAERL QGFPMENVNV VGTYTLRRAV NNDEFLRQAA KVFPYPINII
SGQTEAKTIY AGVCHTQPEK GRKLVIDIGG GSTEMIIGDD FTPLMAESRH MGCVSFATQF
FTDGIISPEN FQRARQSAVN KIEDLGLEYR KLGWQSVLGS SGTIKTVAQV IATNLDPNGT
ITAERLNALI EQTLQAKHFT ELNINGLNQD RVDVFVPGLA ILSAVFDVFH IQQMRYSDGA
LREGVIYSLE KNFQVADIRA STA