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Protein

Manganese-dependent inorganic pyrophosphatase

Gene

ppaC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mn2+Note: Binds 2 manganese ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Manganese 1
Metal bindingi13 – 131Manganese 1
Metal bindingi15 – 151Manganese 2
Metal bindingi75 – 751Manganese 1
Metal bindingi75 – 751Manganese 2
Metal bindingi97 – 971Manganese 2
Metal bindingi149 – 1491Manganese 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU40550-MONOMER.
BRENDAi3.6.1.1. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese-dependent inorganic pyrophosphatase (EC:3.6.1.1)
Alternative name(s):
Pyrophosphate phospho-hydrolase
Short name:
PPase
Gene namesi
Name:ppaC
Ordered Locus Names:BSU40550
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Manganese-dependent inorganic pyrophosphatasePRO_0000158568Add
BLAST

Proteomic databases

PaxDbiP37487.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP37487. 1 interaction.
MINTiMINT-8365645.
STRINGi224308.Bsubs1_010100021886.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi14 – 2916Combined sources
Beta strandi34 – 407Combined sources
Helixi44 – 529Combined sources
Turni65 – 673Combined sources
Beta strandi69 – 757Combined sources
Helixi79 – 813Combined sources
Helixi86 – 883Combined sources
Beta strandi89 – 968Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi115 – 1173Combined sources
Helixi119 – 12911Combined sources
Helixi136 – 15015Combined sources
Turni151 – 1544Combined sources
Helixi160 – 17314Combined sources
Helixi177 – 18711Combined sources
Helixi196 – 1994Combined sources
Turni200 – 2034Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi212 – 22211Combined sources
Helixi224 – 2285Combined sources
Helixi231 – 24414Combined sources
Beta strandi248 – 2569Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2688Combined sources
Turni269 – 2713Combined sources
Helixi272 – 2787Combined sources
Beta strandi286 – 2905Combined sources
Helixi295 – 2984Combined sources
Helixi300 – 3078Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K23X-ray3.00A/B/C/D1-309[»]
1WPMX-ray2.05A/B1-309[»]
1WPNX-ray1.30A/B1-188[»]
2HAWX-ray1.75A/B1-309[»]
2IW4X-ray2.15A/B1-309[»]
ProteinModelPortaliP37487.
SMRiP37487. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37487.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase class C family.Curated

Phylogenomic databases

eggNOGiENOG4105E2M. Bacteria.
COG1227. LUCA.
HOGENOMiHOG000223999.
InParanoidiP37487.
KOiK15986.
OMAiMLCAILS.
OrthoDBiEOG6F81QM.
PhylomeDBiP37487.

Family and domain databases

HAMAPiMF_00207. PPase_C.
InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
IPR022934. Mn-dep_inorganic_PyrPase.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKILIFGHQ NPDTDTICSA IAYADLKNKL GFNAEPVRLG QVNGETQYAL
60 70 80 90 100
DYFKQESPRL VETAANEVNG VILVDHNERQ QSIKDIEEVQ VLEVIDHHRI
110 120 130 140 150
ANFETAEPLY YRAEPVGCTA TILNKMYKEN NVKIEKEIAG LMLSAIISDS
160 170 180 190 200
LLFKSPTCTD QDVAAAKELA EIAGVDAEEY GLNMLKAGAD LSKKTVEELI
210 220 230 240 250
SLDAKEFTLG SKKVEIAQVN TVDIEDVKKR QAELEAVISK VVAEKNLDLF
260 270 280 290 300
LLVITDILEN DSLALAIGNE AAKVEKAFNV TLENNTALLK GVVSRKKQVV

PVLTDAMAE
Length:309
Mass (Da):33,989
Last modified:October 1, 1994 - v1
Checksum:i5C27CCC20D71B941
GO

Mass spectrometryi

Molecular mass is 34019 Da from positions 1 - 309. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05186.1.
AL009126 Genomic DNA. Translation: CAB16092.1.
PIRiS65980.
RefSeqiNP_391935.1. NC_000964.3.
WP_003226902.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB16092; CAB16092; BSU40550.
GeneIDi937817.
KEGGibsu:BSU40550.
PATRICi18980198. VBIBacSub10457_4257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05186.1.
AL009126 Genomic DNA. Translation: CAB16092.1.
PIRiS65980.
RefSeqiNP_391935.1. NC_000964.3.
WP_003226902.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K23X-ray3.00A/B/C/D1-309[»]
1WPMX-ray2.05A/B1-309[»]
1WPNX-ray1.30A/B1-188[»]
2HAWX-ray1.75A/B1-309[»]
2IW4X-ray2.15A/B1-309[»]
ProteinModelPortaliP37487.
SMRiP37487. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37487. 1 interaction.
MINTiMINT-8365645.
STRINGi224308.Bsubs1_010100021886.

Proteomic databases

PaxDbiP37487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16092; CAB16092; BSU40550.
GeneIDi937817.
KEGGibsu:BSU40550.
PATRICi18980198. VBIBacSub10457_4257.

Phylogenomic databases

eggNOGiENOG4105E2M. Bacteria.
COG1227. LUCA.
HOGENOMiHOG000223999.
InParanoidiP37487.
KOiK15986.
OMAiMLCAILS.
OrthoDBiEOG6F81QM.
PhylomeDBiP37487.

Enzyme and pathway databases

BioCyciBSUB:BSU40550-MONOMER.
BRENDAi3.6.1.1. 658.

Miscellaneous databases

EvolutionaryTraceiP37487.

Family and domain databases

HAMAPiMF_00207. PPase_C.
InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
IPR022934. Mn-dep_inorganic_PyrPase.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
    Ogasawara N., Nakai S., Yoshikawa H.
    DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Bacillus subtilis ORF yybQ encodes a manganese-dependent inorganic pyrophosphatase with distinctive properties: the first of a new class of soluble pyrophosphatase?"
    Young T.W., Kuhn N.J., Wadeson A., Ward S., Burges D., Cooke G.D.
    Microbiology 144:2563-2571(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15, CHARACTERIZATION, MASS SPECTROMETRY.
    Strain: WB600.
  4. "Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes."
    Shintani T., Uchiumi T., Yonezawa T., Salminen A., Baykov A.A., Lahti R., Hachimori A.
    FEBS Lett. 439:263-266(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "The 'open' and 'closed' structures of the type-C inorganic pyrophosphatases from Bacillus subtilis and Streptococcus gordonii."
    Ahn S., Milner A.J., Fuetterer K., Konopka M., Ilias M., Young T.W., White S.A.
    J. Mol. Biol. 313:797-811(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiPPAC_BACSU
AccessioniPrimary (citable) accession number: P37487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.