PRSW_BACSU
ID PRSW_BACSU Reviewed; 218 AA.
AC P50738; P94450;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
DE AltName: Full=Protease responsible for activating sigma-W;
DE AltName: Full=Site-1 protease PrsW {ECO:0000305};
DE Short=S1P protease PrsW;
GN Name=prsW {ECO:0000303|PubMed:16816000}; Synonyms=ypdC;
GN OrderedLocusNames=BSU22940;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-218.
RC STRAIN=168;
RX PubMed=8830707; DOI=10.1128/jb.178.20.6059-6063.1996;
RA Moriyama R., Hattori A., Miyata S., Kudoh S., Makino S.;
RT "A gene (sleB) encoding a spore cortex-lytic enzyme from Bacillus subtilis
RT and response of the enzyme to L-alanine-mediated germination.";
RL J. Bacteriol. 178:6059-6063(1996).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLU-95; 75-GLU-GLU-76 AND HIS-175.
RX PubMed=16816000; DOI=10.1101/gad.1440606;
RA Ellermeier C.D., Losick R.;
RT "Evidence for a novel protease governing regulated intramembrane
RT proteolysis and resistance to antimicrobial peptides in Bacillus
RT subtilis.";
RL Genes Dev. 20:1911-1922(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TOPOLOGY.
RC STRAIN=1012;
RX PubMed=17020587; DOI=10.1111/j.1365-2958.2006.05391.x;
RA Heinrich J., Wiegert T.;
RT "YpdC determines site-1 degradation in regulated intramembrane proteolysis
RT of the RsiW anti-sigma factor of Bacillus subtilis.";
RL Mol. Microbiol. 62:566-579(2006).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 75-GLU-GLU-76.
RC STRAIN=1012;
RX PubMed=19889088; DOI=10.1111/j.1365-2958.2009.06940.x;
RA Heinrich J., Hein K., Wiegert T.;
RT "Two proteolytic modules are involved in regulated intramembrane
RT proteolysis of Bacillus subtilis RsiW.";
RL Mol. Microbiol. 74:1412-1426(2009).
CC -!- FUNCTION: Involved in the degradation of anti-sigma-W factor RsiW.
CC Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This
CC results, after two other proteolytic steps catalyzed by the RasP and
CC ClpXP proteases, in the release of SigW and the transcription
CC activation of the genes under the control of the sigma-W factor. Seems
CC to be responsible for sensing antimicrobial peptides that damage the
CC cell membrane and other agents that cause cell envelope stress.
CC Therefore it is a protease governing regulated intramembrane
CC proteolysis and resistance to antimicrobial peptides in B.subtilis.
CC {ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:17020587,
CC ECO:0000269|PubMed:19889088}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17020587};
CC Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Loss of expression of the SigW regulon
CC (PubMed:17020587). {ECO:0000269|PubMed:17020587}.
CC -!- SIMILARITY: Belongs to the protease PrsW family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11472.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L47648; AAC83956.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14210.1; -; Genomic_DNA.
DR EMBL; D79978; BAA11472.1; ALT_FRAME; Genomic_DNA.
DR PIR; B69934; B69934.
DR PIR; T44769; T44769.
DR RefSeq; NP_390175.1; NC_000964.3.
DR RefSeq; WP_003230542.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P50738; -.
DR STRING; 224308.BSU22940; -.
DR MEROPS; M82.001; -.
DR TCDB; 9.B.217.1.1; the transmembrane prsw protease (prsw) family.
DR PaxDb; P50738; -.
DR PRIDE; P50738; -.
DR EnsemblBacteria; CAB14210; CAB14210; BSU_22940.
DR GeneID; 938978; -.
DR KEGG; bsu:BSU22940; -.
DR PATRIC; fig|224308.179.peg.2501; -.
DR eggNOG; COG2339; Bacteria.
DR InParanoid; P50738; -.
DR OMA; DEPYDGI; -.
DR PhylomeDB; P50738; -.
DR BioCyc; BSUB:BSU22940-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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR023596; Peptidase_PrsW_arch/bac.
DR InterPro; IPR026898; PrsW.
DR PANTHER; PTHR36844; PTHR36844; 1.
DR Pfam; PF13367; PrsW-protease; 1.
DR PIRSF; PIRSF016933; PrsW; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="Protease PrsW"
FT /id="PRO_0000049686"
FT TRANSMEM 1..23
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TOPO_DOM 24..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TOPO_DOM 54..98
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TOPO_DOM 122..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TOPO_DOM 152..180
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17020587"
FT TOPO_DOM 204..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17020587"
FT SITE 23
FT /note="Involved in sensing cell envelope stress"
FT /evidence="ECO:0000269|PubMed:16816000"
FT SITE 28
FT /note="Involved in sensing cell envelope stress"
FT /evidence="ECO:0000269|PubMed:16816000"
FT SITE 95
FT /note="Involved in sensing cell envelope stress"
FT /evidence="ECO:0000269|PubMed:16816000"
FT MUTAGEN 75..76
FT /note="EE->AA: Loss of RsiW cleavage activity."
FT /evidence="ECO:0000269|PubMed:16816000,
FT ECO:0000269|PubMed:19889088"
FT MUTAGEN 95
FT /note="E->K: Constitutively active; causes constitutive
FT activation of SigW."
FT /evidence="ECO:0000269|PubMed:16816000"
FT MUTAGEN 175
FT /note="H->A: Loss of RsiW cleavage activity."
FT /evidence="ECO:0000269|PubMed:16816000"
SQ SEQUENCE 218 AA; 24719 MW; 88556D50863E14BC CRC64;
MFAIISAGIA PGIALLSYFY LKDQYDNEPV HMVLRSFFLG VVLVFPIMFI QYVLEKENVG
GGSFFVSFLS SGFLEESLKW FILMISVYPH AHFDEHYDGI VYGASVSLGF ATLENILYLI
GHGVEHAFVR ALLPVSCHAL IGVIMGFYLG KARFSADKAR VKWLTLSLVV PSLLHGSYDF
ILTALSNWIY YMLPFMVFLW WFGLRKAKKA RSVNMMQV
