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Protein

Regulator of sigma-W protease RasP

Gene

rasP

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

Functioni

Is responsible for Site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.2 Publications

Cofactori

Zn2+Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201Zinc; catalyticPROSITE-ProRule annotation
Active sitei21 – 211PROSITE-ProRule annotation
Metal bindingi24 – 241Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU16560-MONOMER.

Protein family/group databases

MEROPSiM50.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of sigma-W protease RasP (EC:3.4.24.-)
Alternative name(s):
Regulating anti-sigma-W factor activity protease
S2P endopeptidase
Site-2 protease RseP
Short name:
S2P protease RseP
Site-2-type intramembrane protease
Zinc metalloprotease RasP
Gene namesi
Name:rasP
Synonyms:yluC
Ordered Locus Names:BSU16560
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei6 – 2621HelicalSequence analysisAdd
BLAST
Transmembranei175 – 19521HelicalSequence analysisAdd
BLAST
Transmembranei346 – 36621HelicalSequence analysisAdd
BLAST
Transmembranei394 – 41421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No cleavage of signal peptides.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211E → A: Loss of signal peptide processing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Regulator of sigma-W protease RasPPRO_0000088429Add
BLAST

Proteomic databases

PaxDbiO31754.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009126.

Structurei

3D structure databases

ProteinModelPortaliO31754.
SMRiO31754. Positions 202-272, 349-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini186 – 27186PDZAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M50B family.Curated
Contains 1 PDZ (DHR) domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DZP. Bacteria.
COG0750. LUCA.
HOGENOMiHOG000006282.
InParanoidiO31754.
KOiK11749.
OMAiQMIVGKR.
OrthoDBiEOG66F07W.
PhylomeDBiO31754.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR004387. Pept_M50_Zn.
IPR008915. Peptidase_M50.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
PF02163. Peptidase_M50. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
TIGRFAMsiTIGR00054. TIGR00054. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVNTVIAFI IIFGTLVFFH ELGHLLLAQR AGILCREFAI GFGPKIFSFK
60 70 80 90 100
KNETVYTIRL LPVGGFVRMA GEDPEMIEVK PGYTVGLLFN KEDQVEKVII
110 120 130 140 150
NQKEKYPDAL VIEVETADLE HDMKITGYEQ GKEDELSSFT VSETSFFIVD
160 170 180 190 200
GEEVQIAPYN RQFGSKPVWQ RIKAIAAGPI MNFILAYVIL VMLGLIQGVP
210 220 230 240 250
SNEPMLGQLT DNGRAAEAGL KEGDYIQSIN GEKMRSWTDI VSAVKENPEK
260 270 280 290 300
EMDVAVKRDN KTLHISVTPE AVKDENKKTI GRFGSYAPTE KGVLSAVAYG
310 320 330 340 350
ATSTVDVTKA ILTNLSKLVT GQFKLDMLSG PVGIYDMTDQ VAKTGIVNLF
360 370 380 390 400
QFAAFLSINL GIVNLLPIPA LDGGRLLFLF IEAIRGKPIN REKEAFVVFI
410 420
GVAFLMLLML VVTWNDIQRL FL
Length:422
Mass (Da):46,744
Last modified:January 1, 1998 - v1
Checksum:i30817108B49FAEA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13529.1.
PIRiC69881.
RefSeqiNP_389538.1. NC_000964.3.
WP_010886508.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13529; CAB13529; BSU16560.
GeneIDi939612.
KEGGibsu:BSU16560.
PATRICi18975119. VBIBacSub10457_1751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13529.1.
PIRiC69881.
RefSeqiNP_389538.1. NC_000964.3.
WP_010886508.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO31754.
SMRiO31754. Positions 202-272, 349-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009126.

Protein family/group databases

MEROPSiM50.004.

Proteomic databases

PaxDbiO31754.

Protocols and materials databases

DNASUi939612.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13529; CAB13529; BSU16560.
GeneIDi939612.
KEGGibsu:BSU16560.
PATRICi18975119. VBIBacSub10457_1751.

Phylogenomic databases

eggNOGiENOG4105DZP. Bacteria.
COG0750. LUCA.
HOGENOMiHOG000006282.
InParanoidiO31754.
KOiK11749.
OMAiQMIVGKR.
OrthoDBiEOG66F07W.
PhylomeDBiO31754.

Enzyme and pathway databases

BioCyciBSUB:BSU16560-MONOMER.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR004387. Pept_M50_Zn.
IPR008915. Peptidase_M50.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
PF02163. Peptidase_M50. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
TIGRFAMsiTIGR00054. TIGR00054. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC."
    Schoebel S., Zellmeier S., Schumann W., Wiegert T.
    Mol. Microbiol. 52:1091-1105(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RSIW DEGRADATION.
  3. "Involvement of Clp protease activity in modulating the Bacillus subtilis sigma-W stress response."
    Zellmeier S., Schumann W., Wiegert T.
    Mol. Microbiol. 61:1569-1582(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
  4. "Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria."
    Saito A., Hizukuri Y., Matsuo E., Chiba S., Mori H., Nishimura O., Ito K., Akiyama Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:13740-13745(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF SIGNAL PEPTIDES, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-21.
    Strain: 168 / PY79.

Entry informationi

Entry nameiRASP_BACSU
AccessioniPrimary (citable) accession number: O31754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Peptidase families
    Classification of peptidase families and list of entries
  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.