PPAC_STRMU
ID PPAC_STRMU Reviewed; 310 AA.
AC O68579;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
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; Synonyms=dlt5, ppx1; OrderedLocusNames=SMU_1687;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RX PubMed=11029425; DOI=10.1128/jb.182.21.6055-6065.2000;
RA Boyd D.A., Cvitkovitch D.G., Bleiweis A.S., Kiriukhin M.Y., Debabov D.V.,
RA Neuhaus F.C., Hamilton I.R.;
RT "Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans
RT results in acid sensitivity.";
RL J. Bacteriol. 182:6055-6065(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Spatafora G.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11525166; DOI=10.1016/s0969-2126(01)00587-1;
RA Merckel M.C., Fabrichniy I.P., Salminen A., Kalkkinen N., Baykov A.A.,
RA Lahti R., Goldman A.;
RT "Crystal structure of Streptococcus mutans pyrophosphatase: a new fold for
RT an old mechanism.";
RL Structure 9:289-297(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; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
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; AF051356; AAC05778.1; -; Genomic_DNA.
DR EMBL; AF050517; AAC29042.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59324.1; -; Genomic_DNA.
DR RefSeq; NP_722018.1; NC_004350.2.
DR RefSeq; WP_002262586.1; NC_004350.2.
DR PDB; 1I74; X-ray; 2.20 A; A/B=2-310.
DR PDBsum; 1I74; -.
DR AlphaFoldDB; O68579; -.
DR SMR; O68579; -.
DR STRING; 210007.SMU_1687; -.
DR PRIDE; O68579; -.
DR EnsemblBacteria; AAN59324; AAN59324; SMU_1687.
DR KEGG; smu:SMU_1687; -.
DR PATRIC; fig|210007.7.peg.1507; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_0_1_9; -.
DR OMA; IMLCAIL; -.
DR PhylomeDB; O68579; -.
DR EvolutionaryTrace; O68579; -.
DR Proteomes; UP000002512; 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..310
FT /note="Probable manganese-dependent inorganic
FT pyrophosphatase"
FT /id="PRO_0000158590"
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 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1I74"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:1I74"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:1I74"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:1I74"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:1I74"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:1I74"
SQ SEQUENCE 310 AA; 33403 MW; 307A318A2A1CEA71 CRC64;
MSKILVFGHQ NPDSDAIGSS MAYAYLKRQL GVDAQAVALG NPNEETAFVL DYFGIQAPPV
VKSAQAEGAK QVILTDHNEF QQSIADIREV EVVEVVDHHR VANFETANPL YMRLEPVGSA
SSIVYRLYKE NGVAIPKEIA GVMLSGLISD TLLLKSPTTH ASDPAVAEDL AKIAGVDLQE
YGLAMLKAGT NLASKTAAQL VDIDAKTFEL NGSQVRVAQV NTVDINEVLE RQNEIEEAIK
ASQAANGYSD FVLMITDILN SNSEILALGN NTDKVEAAFN FTLKNNHAFL AGAVSRKKQV
VPQLTESFNG
