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PPAC_BACCZ
ID   PPAC_BACCZ              Reviewed;         309 AA.
AC   Q63AC7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=BCE33L2551;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000255|HAMAP-
CC       Rule:MF_00207}.
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DR   EMBL; CP000001; AAU17708.1; -; Genomic_DNA.
DR   RefSeq; WP_000416876.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q63AC7; -.
DR   SMR; Q63AC7; -.
DR   EnsemblBacteria; AAU17708; AAU17708; BCE33L2551.
DR   KEGG; bcz:BCE33L2551; -.
DR   PATRIC; fig|288681.22.peg.2921; -.
DR   OMA; IMLCAIL; -.
DR   Proteomes; UP000002612; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..309
FT                   /note="Probable manganese-dependent inorganic
FT                   pyrophosphatase"
FT                   /id="PRO_1000012308"
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         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         97
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
SQ   SEQUENCE   309 AA;  33748 MW;  C37016E6AA82799A CRC64;
     MEKVLVFGHK NPDTDAICSA IAYAELKKEL GMNAEPVRLG EISGETQFAL NYFKVEGPRF
     VETVANEVDN VILVDHNERQ QSANDIESVR VLEVIDHHRI ANFETSDPIY YRCEPVGCTA
     TILNKMYKEN GVTIRKEVAG LMLSAIISDS LLFKSPTCTE QDVAAARELA EIAGVDADKY
     GLEMLKAGAD LSGKTMEQLI SLDAKEFQMG NAKVEIAQVN AVDTNDVLVH QAELEKVISA
     VVEEKGLDLF LFVVTDILTN DSVGLAIGKA ANIVEKAYNV SLENNTATLK GVVSRKKQIV
     PVLTEAFQA
 
 
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