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O34779 (PRPC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase PrpC

EC=3.1.3.16
Gene names
Name:prpC
Synonyms:yloO
Ordered Locus Names:BSU15760
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Function

Protein phosphatase that dephosphorylates PrkC and FusA (elongation factor G). PrpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Ref.3 Ref.4 Ref.5

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit. Ref.3

Sequence similarities

Contains 1 PP2C-like domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Protein phosphatase PrpC
PRO_0000253340

Regions

Domain2 – 236235PP2C-like

Sites

Metal binding361Manganese 1 By similarity
Metal binding361Manganese 2 By similarity
Metal binding371Manganese 1; via carbonyl oxygen By similarity
Metal binding1951Manganese 2 By similarity
Metal binding2341Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O34779 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A01A30A97B47C86E

FASTA25427,674
        10         20         30         40         50         60 
MLTALKTDTG KIRQHNEDDA GIFKGKDEFI LAVVADGMGG HLAGDVASKM AVKAMGEKWN 

        70         80         90        100        110        120 
EAETIPTAPS ECEKWLIEQI LSVNSKIYDH AQAHEECQGM GTTIVCALFT GKTVSVAHIG 

       130        140        150        160        170        180 
DSRCYLLQDD DFVQVTEDHS LVNELVRTGE ISREDAEHHP RKNVLTKALG TDQLVSIDTR 

       190        200        210        220        230        240 
SFDIEPGDKL LLCSDGLTNK VEGTELKDIL QSDSAPQEKV NLLVDKANQN GGEDNITAVL 

       250 
LELALQVEEG EDQC 

« Hide

References

« Hide 'large scale' references
[1]"A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
Foulger D., Errington J.
Microbiology 144:801-805(1998) [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. expand/collapse author list , 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]"Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family."
Obuchowski M., Madec E., Delattre D., Boel G., Iwanicki A., Foulger D., Seror S.J.
J. Bacteriol. 182:5634-5638(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR.
Strain: 168.
[4]"Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes."
Madec E., Laszkiewicz A., Iwanicki A., Obuchowski M., Seror S.
Mol. Microbiol. 46:571-586(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 168.
[5]"The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells."
Gaidenko T.A., Kim T.-J., Price C.W.
J. Bacteriol. 184:6109-6114(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION OF SUBSTRATES.
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13937 Genomic DNA. Translation: CAA74266.1.
AL009126 Genomic DNA. Translation: CAB13449.1.
PIRG69878.
RefSeqNP_389458.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34779.
SMRO34779. Positions 1-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO34779. 1 interaction.
STRING224308.BSU15760.

Protein family/group databases

PptaseDBP3D040488.

Proteomic databases

PaxDbO34779.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13449; CAB13449; BSU15760.
GeneID935931.
KEGGbsu:BSU15760.
PATRIC18974959. VBIBacSub10457_1671.

Organism-specific databases

GenoListBSU15760. [Micado]

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000235782.
KOK01090.
OMAFFIVADG.
OrthoDBEOG65N17S.
ProtClustDBCLSK887289.

Enzyme and pathway databases

BioCycBSUB:BSU15760-MONOMER.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
ProtoNetSearch...

Entry information

Entry namePRPC_BACSU
AccessionPrimary (citable) accession number: O34779
Secondary accession number(s): Q799K9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList