PPAC_STRA5
ID PPAC_STRA5 Reviewed; 311 AA.
AC Q8DYS6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable manganese-dependent inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00207};
DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00207};
DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00207};
DE Short=PPase {ECO:0000255|HAMAP-Rule:MF_00207};
GN Name=ppaC {ECO:0000255|HAMAP-Rule:MF_00207}; Synonyms=ppa;
GN OrderedLocusNames=SAG1397;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
RN [2]
RP PHOSPHORYLATION.
RX PubMed=12562757; DOI=10.1074/jbc.m212747200;
RA Rajagopal L., Clancy A., Rubens C.E.;
RT "A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus
RT agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect
RT growth, cell segregation, and virulence.";
RL J. Biol. Chem. 278:14429-14441(2003).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00207};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00207};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00207};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00207}.
CC -!- PTM: Phosphorylated on serine residue(s) by stk1. Dephosphorylated by
CC stp1. {ECO:0000269|PubMed:12562757}.
CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000255|HAMAP-
CC Rule:MF_00207}.
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DR EMBL; AE009948; AAN00268.1; -; Genomic_DNA.
DR RefSeq; NP_688395.1; NC_004116.1.
DR RefSeq; WP_000036019.1; NC_004116.1.
DR PDB; 2ENX; X-ray; 2.80 A; A/B=2-311.
DR PDBsum; 2ENX; -.
DR AlphaFoldDB; Q8DYS6; -.
DR SMR; Q8DYS6; -.
DR STRING; 208435.SAG1397; -.
DR EnsemblBacteria; AAN00268; AAN00268; SAG1397.
DR KEGG; sag:SAG1397; -.
DR PATRIC; fig|208435.3.peg.1405; -.
DR HOGENOM; CLU_025243_0_1_9; -.
DR OMA; IMLCAIL; -.
DR BRENDA; 3.6.1.1; 5917.
DR EvolutionaryTrace; Q8DYS6; -.
DR Proteomes; UP000000821; 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 Phosphoprotein; Reference proteome.
FT CHAIN 1..311
FT /note="Probable manganese-dependent inorganic
FT pyrophosphatase"
FT /id="PRO_0000158588"
FT BINDING 9
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
SQ SEQUENCE 311 AA; 33597 MW; 281CB9BEC345EAB0 CRC64;
MSKILVFGHQ NPDSDAIGSS VAFAYLAKEA WGLDTEAVAL GTPNEETAYV LDYFGVQAPR
VVESAKAEGV ETVILTDHNE FQQSISDIKD VTVYGVVDHH RVANFETANP LYMRLEPVGS
ASSIVYRMFK ENGVSVPKEL AGLLLSGLIS DTLLLKSPTT HASDIPVAKE LAELAGVNLE
EYGLEMLKAG TNLSSKTAAE LIDIDAKTFE LNGEAVRVAQ VNTVDINDIL ARQEEIEVAI
QEAIVTEGYS DFVLMITDIV NSNSEILALG SNMAKVEAAF EFTLENNHAF LAGAVSRKKQ
VVPQLTESYN A
