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O34779

- PRPC_BACSU

UniProt

O34779 - PRPC_BACSU

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Protein
Protein phosphatase PrpC
Gene
prpC, yloO, BSU15760
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Protein predictedi

Functioni

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.3 Publications

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Manganese 1 By similarity
Metal bindingi36 – 361Manganese 2 By similarity
Metal bindingi37 – 371Manganese 1; via carbonyl oxygen By similarity
Metal bindingi195 – 1951Manganese 2 By similarity
Metal bindingi234 – 2341Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU15760-MONOMER.

Protein family/group databases

PptaseDBiP3D040488.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase PrpC (EC:3.1.3.16)
Gene namesi
Name:prpC
Synonyms:yloO
Ordered Locus Names:BSU15760
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU15760. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Protein phosphatase PrpC
PRO_0000253340Add
BLAST

Proteomic databases

PaxDbiO34779.

Interactioni

Protein-protein interaction databases

IntActiO34779. 1 interaction.
STRINGi224308.BSU15760.

Structurei

3D structure databases

ProteinModelPortaliO34779.
SMRiO34779. Positions 1-244.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 236235PP2C-like
Add
BLAST

Sequence similaritiesi

Contains 1 PP2C-like domain.

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000235782.
KOiK01090.
OMAiHEECQGM.
OrthoDBiEOG65N17S.
PhylomeDBiO34779.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.

Sequencei

Sequence statusi: Complete.

O34779-1 [UniParc]FASTAAdd to Basket

« Hide

MLTALKTDTG KIRQHNEDDA GIFKGKDEFI LAVVADGMGG HLAGDVASKM    50
AVKAMGEKWN EAETIPTAPS ECEKWLIEQI LSVNSKIYDH AQAHEECQGM 100
GTTIVCALFT GKTVSVAHIG DSRCYLLQDD DFVQVTEDHS LVNELVRTGE 150
ISREDAEHHP RKNVLTKALG TDQLVSIDTR SFDIEPGDKL LLCSDGLTNK 200
VEGTELKDIL QSDSAPQEKV NLLVDKANQN GGEDNITAVL LELALQVEEG 250
EDQC 254
Length:254
Mass (Da):27,674
Last modified:January 1, 1998 - v1
Checksum:iA01A30A97B47C86E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13937 Genomic DNA. Translation: CAA74266.1.
AL009126 Genomic DNA. Translation: CAB13449.1.
PIRiG69878.
RefSeqiNP_389458.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13449; CAB13449; BSU15760.
GeneIDi935931.
KEGGibsu:BSU15760.
PATRICi18974959. VBIBacSub10457_1671.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13937 Genomic DNA. Translation: CAA74266.1 .
AL009126 Genomic DNA. Translation: CAB13449.1 .
PIRi G69878.
RefSeqi NP_389458.1. NC_000964.3.

3D structure databases

ProteinModelPortali O34779.
SMRi O34779. Positions 1-244.
ModBasei Search...

Protein-protein interaction databases

IntActi O34779. 1 interaction.
STRINGi 224308.BSU15760.

Protein family/group databases

PptaseDBi P3D040488.

Proteomic databases

PaxDbi O34779.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13449 ; CAB13449 ; BSU15760 .
GeneIDi 935931.
KEGGi bsu:BSU15760.
PATRICi 18974959. VBIBacSub10457_1671.

Organism-specific databases

GenoListi BSU15760. [Micado ]

Phylogenomic databases

eggNOGi COG0631.
HOGENOMi HOG000235782.
KOi K01090.
OMAi HEECQGM.
OrthoDBi EOG65N17S.
PhylomeDBi O34779.

Enzyme and pathway databases

BioCyci BSUB:BSU15760-MONOMER.

Family and domain databases

Gene3Di 3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81606. SSF81606. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPRPC_BACSU
AccessioniPrimary (citable) accession number: O34779
Secondary accession number(s): Q799K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 89 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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