ID   PPAC_STRGC              Reviewed;         311 AA.
AC   P95765; A8AYR5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Probable manganese-dependent inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=ppaC; OrderedLocusNames=SGO_1648;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8926080; DOI=10.1128/iai.64.10.4137-4142.1996;
RA   Whittaker C.J., Clemans D.L., Kolenbrander P.E.;
RT   "Insertional inactivation of an intrageneric coaggregation-relevant adhesin
RT   locus from Streptococcus gordonii DL1 (Challis).";
RL   Infect. Immun. 64:4137-4142(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=11697905; DOI=10.1006/jmbi.2001.5070;
RA   Ahn S., Milner A.J., Fuetterer K., Konopka M., Ilias M., Young T.W.,
RA   White S.A.;
RT   "The 'open' and 'closed' structures of the type-C inorganic
RT   pyrophosphatases from Bacillus subtilis and Streptococcus gordonii.";
RL   J. Mol. Biol. 313:797-811(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 manganese ions per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR   EMBL; U57759; AAB39104.1; -; Genomic_DNA.
DR   EMBL; CP000725; ABV09962.1; -; Genomic_DNA.
DR   RefSeq; WP_012130706.1; NC_009785.1.
DR   PDB; 1K20; X-ray; 1.50 A; A/B=2-311.
DR   PDB; 1WPP; X-ray; 2.05 A; A/B=1-311.
DR   PDBsum; 1K20; -.
DR   PDBsum; 1WPP; -.
DR   AlphaFoldDB; P95765; -.
DR   SMR; P95765; -.
DR   STRING; 467705.SGO_1648; -.
DR   EnsemblBacteria; ABV09962; ABV09962; SGO_1648.
DR   KEGG; sgo:SGO_1648; -.
DR   eggNOG; COG1227; Bacteria.
DR   HOGENOM; CLU_025243_0_1_9; -.
DR   OMA; IMLCAIL; -.
DR   BRENDA; 3.6.1.1; 5934.
DR   EvolutionaryTrace; P95765; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.20; -; 1.
DR   HAMAP; MF_00207; PPase_C; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   InterPro; IPR022934; Mn-dep_inorganic_PyrPase.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; SSF64182; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..311
FT                   /note="Probable manganese-dependent inorganic
FT                   pyrophosphatase"
FT                   /id="PRO_0000158589"
FT   BINDING         9
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   BINDING         99
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   BINDING         151
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           14..31
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           45..54
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          91..98
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           121..131
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           138..152
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   TURN            153..156
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           162..175
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           179..188
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          204..211
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          214..224
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           226..230
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           233..247
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          250..258
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          263..271
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           273..280
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   STRAND          288..292
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           297..300
FT                   /evidence="ECO:0007829|PDB:1K20"
FT   HELIX           302..310
FT                   /evidence="ECO:0007829|PDB:1K20"
SQ   SEQUENCE   311 AA;  33541 MW;  610A704B681E2889 CRC64;
     MSKILVFGHQ NPDSDAIGSS YAFAYLAREA YGLDTEAVAL GEPNEETAFV LDYFGVAAPR
     VITSAKAEGA EQVILTDHNE FQQSVADIAE VEVYGVVDHH RVANFETANP LYMRLEPVGS
     ASSIVYRMFK EHSVAVSKEI AGLMLSGLIS DTLLLKSPTT HPTDKAIAPE LAELAGVNLE
     EYGLAMLKAG TNLASKSAEE LIDIDAKTFE LNGNNVRVAQ VNTVDIAEVL ERQAEIEAAI
     EKAIADNGYS DFVLMITDII NSNSEILAIG SNMDKVEAAF NFVLENNHAF LAGAVSRKKQ
     VVPQLTESFN A