PPAC_BACSU
ID PPAC_BACSU Reviewed; 309 AA.
AC P37487;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Manganese-dependent inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=ppaC; OrderedLocusNames=BSU40550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1-15, CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=WB600;
RX PubMed=9782505; DOI=10.1099/00221287-144-9-2563;
RA Young T.W., Kuhn N.J., Wadeson A., Ward S., Burges D., Cooke G.D.;
RT "Bacillus subtilis ORF yybQ encodes a manganese-dependent inorganic
RT pyrophosphatase with distinctive properties: the first of a new class of
RT soluble pyrophosphatase?";
RL Microbiology 144:2563-2571(1998).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9845334; DOI=10.1016/s0014-5793(98)01381-7;
RA Shintani T., Uchiumi T., Yonezawa T., Salminen A., Baykov A.A., Lahti R.,
RA Hachimori A.;
RT "Cloning and expression of a unique inorganic pyrophosphatase from Bacillus
RT subtilis: evidence for a new family of enzymes.";
RL FEBS Lett. 439:263-266(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 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.
CC -!- MASS SPECTROMETRY: Mass=34019; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9782505};
CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR EMBL; D26185; BAA05186.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16092.1; -; Genomic_DNA.
DR PIR; S65980; S65980.
DR RefSeq; NP_391935.1; NC_000964.3.
DR RefSeq; WP_003226902.1; NZ_JNCM01000034.1.
DR PDB; 1K23; X-ray; 3.00 A; A/B/C/D=1-309.
DR PDB; 1WPM; X-ray; 2.05 A; A/B=1-309.
DR PDB; 1WPN; X-ray; 1.30 A; A/B=1-188.
DR PDB; 2HAW; X-ray; 1.75 A; A/B=1-309.
DR PDB; 2IW4; X-ray; 2.15 A; A/B=1-309.
DR PDBsum; 1K23; -.
DR PDBsum; 1WPM; -.
DR PDBsum; 1WPN; -.
DR PDBsum; 2HAW; -.
DR PDBsum; 2IW4; -.
DR AlphaFoldDB; P37487; -.
DR SMR; P37487; -.
DR IntAct; P37487; 1.
DR MINT; P37487; -.
DR STRING; 224308.BSU40550; -.
DR jPOST; P37487; -.
DR PaxDb; P37487; -.
DR PRIDE; P37487; -.
DR EnsemblBacteria; CAB16092; CAB16092; BSU_40550.
DR GeneID; 937817; -.
DR KEGG; bsu:BSU40550; -.
DR PATRIC; fig|224308.179.peg.4391; -.
DR eggNOG; COG1227; Bacteria.
DR InParanoid; P37487; -.
DR OMA; IMLCAIL; -.
DR PhylomeDB; P37487; -.
DR BioCyc; BSUB:BSU40550-MON; -.
DR BRENDA; 3.6.1.1; 658.
DR EvolutionaryTrace; P37487; -.
DR PRO; PR:P37487; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..309
FT /note="Manganese-dependent inorganic pyrophosphatase"
FT /id="PRO_0000158568"
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 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:1WPN"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1WPN"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1WPN"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1WPN"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1WPN"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1WPN"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:1WPN"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:1WPN"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2HAW"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:2HAW"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2HAW"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:2HAW"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:2HAW"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:2HAW"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:2HAW"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:2HAW"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:2HAW"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:2HAW"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:2HAW"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:2HAW"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2HAW"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:2HAW"
SQ SEQUENCE 309 AA; 33989 MW; 5C27CCC20D71B941 CRC64;
MEKILIFGHQ NPDTDTICSA IAYADLKNKL GFNAEPVRLG QVNGETQYAL DYFKQESPRL
VETAANEVNG VILVDHNERQ QSIKDIEEVQ VLEVIDHHRI ANFETAEPLY YRAEPVGCTA
TILNKMYKEN NVKIEKEIAG LMLSAIISDS LLFKSPTCTD QDVAAAKELA EIAGVDAEEY
GLNMLKAGAD LSKKTVEELI SLDAKEFTLG SKKVEIAQVN TVDIEDVKKR QAELEAVISK
VVAEKNLDLF LLVITDILEN DSLALAIGNE AAKVEKAFNV TLENNTALLK GVVSRKKQVV
PVLTDAMAE
