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Protein

Protein phosphatase PrpC

Gene

prpC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Sites

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

GO - Molecular functioni

GO - Biological processi

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.

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 Componenti: Chromosome

Organism-specific databases

GenoListiBSU15760. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Protein phosphatase PrpCPRO_0000253340Add
BLAST

Proteomic databases

PaxDbiO34779.

Interactioni

Protein-protein interaction databases

IntActiO34779. 1 interaction.
STRINGi224308.Bsubs1_010100008701.

Structurei

3D structure databases

ProteinModelPortaliO34779.
SMRiO34779. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 243242PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000235782.
InParanoidiO34779.
KOiK01090.
OMAiHTWVARA.
OrthoDBiEOG65N17S.
PhylomeDBiO34779.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR001932. PPM-type_phosphatase_dom.
[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.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34779-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTALKTDTG KIRQHNEDDA GIFKGKDEFI LAVVADGMGG HLAGDVASKM
60 70 80 90 100
AVKAMGEKWN EAETIPTAPS ECEKWLIEQI LSVNSKIYDH AQAHEECQGM
110 120 130 140 150
GTTIVCALFT GKTVSVAHIG DSRCYLLQDD DFVQVTEDHS LVNELVRTGE
160 170 180 190 200
ISREDAEHHP RKNVLTKALG TDQLVSIDTR SFDIEPGDKL LLCSDGLTNK
210 220 230 240 250
VEGTELKDIL QSDSAPQEKV NLLVDKANQN GGEDNITAVL LELALQVEEG

EDQC
Length:254
Mass (Da):27,674
Last modified:January 1, 1998 - v1
Checksum:iA01A30A97B47C86E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13937 Genomic DNA. Translation: CAA74266.1.
AL009126 Genomic DNA. Translation: CAB13449.1.
PIRiG69878.
RefSeqiNP_389458.1. NC_000964.3.
WP_003232064.1. NZ_JNCM01000035.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13937 Genomic DNA. Translation: CAA74266.1.
AL009126 Genomic DNA. Translation: CAB13449.1.
PIRiG69878.
RefSeqiNP_389458.1. NC_000964.3.
WP_003232064.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO34779.
SMRiO34779. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO34779. 1 interaction.
STRINGi224308.Bsubs1_010100008701.

Proteomic databases

PaxDbiO34779.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU15760. [Micado]

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000235782.
InParanoidiO34779.
KOiK01090.
OMAiHTWVARA.
OrthoDBiEOG65N17S.
PhylomeDBiO34779.

Enzyme and pathway databases

BioCyciBSUB:BSU15760-MONOMER.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR001932. PPM-type_phosphatase_dom.
[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.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 22, 2015
This is version 98 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

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 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.