RASP_BACSU
ID RASP_BACSU Reviewed; 422 AA.
AC O31754;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Regulator of sigma-W protease RasP;
DE EC=3.4.24.-;
DE AltName: Full=Regulating anti-sigma-W factor activity protease;
DE AltName: Full=S2P endopeptidase;
DE AltName: Full=Site-2 protease RseP;
DE Short=S2P protease RseP;
DE AltName: Full=Site-2-type intramembrane protease;
DE AltName: Full=Zinc metalloprotease RasP;
GN Name=rasP {ECO:0000303|PubMed:16899079}; Synonyms=yluC;
GN OrderedLocusNames=BSU16560;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN RSIW DEGRADATION.
RX PubMed=15130127; DOI=10.1111/j.1365-2958.2004.04031.x;
RA Schoebel S., Zellmeier S., Schumann W., Wiegert T.;
RT "The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by
RT intramembrane proteolysis through YluC.";
RL Mol. Microbiol. 52:1091-1105(2004).
RN [3]
RP GENE NAME.
RX PubMed=16899079; DOI=10.1111/j.1365-2958.2006.05323.x;
RA Zellmeier S., Schumann W., Wiegert T.;
RT "Involvement of Clp protease activity in modulating the Bacillus subtilis
RT sigma-W stress response.";
RL Mol. Microbiol. 61:1569-1582(2006).
RN [4]
RP FUNCTION IN CLEAVAGE OF SIGNAL PEPTIDES, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-21.
RC STRAIN=168 / PY79;
RX PubMed=21810987; DOI=10.1073/pnas.1108376108;
RA Saito A., Hizukuri Y., Matsuo E., Chiba S., Mori H., Nishimura O., Ito K.,
RA Akiyama Y.;
RT "Post-liberation cleavage of signal peptides is catalyzed by the site-2
RT protease (S2P) in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13740-13745(2011).
CC -!- FUNCTION: Is responsible for site-2 cleavage of the RsiW anti-sigma
CC factor (PubMed:15130127). This results, after a third proteolytic step
CC catalyzed by the ClpXP protease, in the release of SigW and the
CC transcription activation of the genes under the control of the sigma-W
CC factor (PubMed:16899079). Can also cleave liberated signal peptides of
CC PenP and Mpr, probably within in the cell membrane (PubMed:21810987).
CC {ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:21810987}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No cleavage of signal peptides.
CC {ECO:0000269|PubMed:21810987}.
CC -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs when an
CC extracytoplasmic signal triggers a concerted proteolytic cascade to
CC transmit information and elicit cellular responses. A membrane-spanning
CC regulatory substrate protein is first cut extracytoplasmically (site-1
CC protease, S1P), then within the membrane itself (site-2 protease, S2P,
CC this enzyme), while cytoplasmic proteases finish degrading the
CC regulatory protein, liberating the effector protein.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13529.1; -; Genomic_DNA.
DR PIR; C69881; C69881.
DR RefSeq; NP_389538.1; NC_000964.3.
DR RefSeq; WP_010886508.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31754; -.
DR SMR; O31754; -.
DR STRING; 224308.BSU16560; -.
DR MEROPS; M50.011; -.
DR TCDB; 9.B.149.2.1; the m50 peptidase (m50-p) family.
DR PaxDb; O31754; -.
DR PRIDE; O31754; -.
DR DNASU; 939612; -.
DR EnsemblBacteria; CAB13529; CAB13529; BSU_16560.
DR GeneID; 939612; -.
DR KEGG; bsu:BSU16560; -.
DR PATRIC; fig|224308.43.peg.1751; -.
DR eggNOG; COG0750; Bacteria.
DR InParanoid; O31754; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; O31754; -.
DR BioCyc; BSUB:BSU16560-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..422
FT /note="Regulator of sigma-W protease RasP"
FT /id="PRO_0000088429"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 186..271
FT /note="PDZ"
FT ACT_SITE 21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT MUTAGEN 21
FT /note="E->A: Loss of signal peptide processing."
FT /evidence="ECO:0000269|PubMed:21810987"
SQ SEQUENCE 422 AA; 46744 MW; 30817108B49FAEA6 CRC64;
MFVNTVIAFI IIFGTLVFFH ELGHLLLAQR AGILCREFAI GFGPKIFSFK KNETVYTIRL
LPVGGFVRMA GEDPEMIEVK PGYTVGLLFN KEDQVEKVII NQKEKYPDAL VIEVETADLE
HDMKITGYEQ GKEDELSSFT VSETSFFIVD GEEVQIAPYN RQFGSKPVWQ RIKAIAAGPI
MNFILAYVIL VMLGLIQGVP SNEPMLGQLT DNGRAAEAGL KEGDYIQSIN GEKMRSWTDI
VSAVKENPEK EMDVAVKRDN KTLHISVTPE AVKDENKKTI GRFGSYAPTE KGVLSAVAYG
ATSTVDVTKA ILTNLSKLVT GQFKLDMLSG PVGIYDMTDQ VAKTGIVNLF QFAAFLSINL
GIVNLLPIPA LDGGRLLFLF IEAIRGKPIN REKEAFVVFI GVAFLMLLML VVTWNDIQRL
FL
