PRSW_CLOD6
ID PRSW_CLOD6 Reviewed; 238 AA.
AC Q188Z4;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
GN Name=prsW; Synonyms=sleB; OrderedLocusNames=CD630_05520;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=630;
RX PubMed=21628514; DOI=10.1128/iai.00019-11;
RA Ho T.D., Ellermeier C.D.;
RT "PrsW is required for colonization, resistance to antimicrobial peptides,
RT and expression of extracytoplasmic function sigma factors in Clostridium
RT difficile.";
RL Infect. Immun. 79:3229-3238(2011).
CC -!- FUNCTION: Involved in the degradation of specific anti-sigma factors,
CC specifically RsiT. Involved in the regulation of extracytoplasmic
CC function sigma factors expression. Seems to play a role in the
CC resistance to antimicrobial peptides. Required for colonization or
CC survival in the host cecum. {ECO:0000269|PubMed:21628514}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced expression of the extracytoplasmic
CC function sigma factor genes csfT and csfU (5-fold in mutant in
CC comparison to wild-type). Decreased virulence (30-fold less virulent
CC than the wild-type). {ECO:0000269|PubMed:21628514}.
CC -!- SIMILARITY: Belongs to the protease PrsW family. {ECO:0000305}.
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DR EMBL; AM180355; CAJ67385.1; -; Genomic_DNA.
DR RefSeq; WP_009901989.1; NZ_CP010905.2.
DR RefSeq; YP_001087028.1; NC_009089.1.
DR AlphaFoldDB; Q188Z4; -.
DR STRING; 272563.CD630_05520; -.
DR TCDB; 9.B.217.1.4; the transmembrane prsw protease (prsw) family.
DR EnsemblBacteria; CAJ67385; CAJ67385; CD630_05520.
DR GeneID; 66353049; -.
DR KEGG; cdf:CD630_05520; -.
DR KEGG; pdc:CDIF630_00665; -.
DR PATRIC; fig|272563.120.peg.562; -.
DR eggNOG; COG2339; Bacteria.
DR OMA; DEPYDGI; -.
DR PhylomeDB; Q188Z4; -.
DR BioCyc; PDIF272563:G12WB-664-MON; -.
DR Proteomes; UP000001978; 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 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..238
FT /note="Protease PrsW"
FT /id="PRO_0000419803"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 238 AA; 27827 MW; 382E00E8BA0D3B1D CRC64;
MKLDLFLLAI IPILIGMFWI RSKDRYCREP LIHLIKFFLI GAFLSVIIIL LENLLMKFNV
FEGYSELIYV SFVVAGLVEE GVKALILIPA LIKEKHFTEK LDGIIYSVFL ALGFATIENM
VYIFSESRNL ALQVGINRAV ISIPAHVMFA ITMGYYISKY KFEGNKNKRR EYLFMAVLIP
ILLHGVFDFI LMIEYRWAII LLIVYVIILW KINLDKLEKY MNHSKKVFFG NLRKKKKK
