(data stored in ACNUC9435 zone)

SWISSPROT: 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   11-DEC-2019, entry version 61.
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; Clostridiales; 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 virulency (30-fold less virulent
CC       than the wild-type). {ECO:0000269|PubMed:21628514}.
CC   -!- SIMILARITY: Belongs to the protease PrsW family. {ECO:0000305}.
DR   EMBL; AM180355; CAJ67385.1; -; Genomic_DNA.
DR   RefSeq; WP_009901989.1; NZ_CP010905.2.
DR   RefSeq; YP_001087028.1; NC_009089.1.
DR   STRING; 272563.CD630_05520; -.
DR   MEROPS; M82.001; -.
DR   TCDB; 9.B.217.1.4; the transmembrane prsw protease (prsw) family.
DR   PRIDE; Q188Z4; -.
DR   EnsemblBacteria; CAJ67385; CAJ67385; CD630_05520.
DR   GeneID; 4916687; -.
DR   KEGG; cdf:CD630_05520; -.
DR   KEGG; pdc:CDIF630_00665; -.
DR   PATRIC; fig|272563.120.peg.562; -.
DR   eggNOG; ENOG4108PNU; Bacteria.
DR   eggNOG; COG2339; LUCA.
DR   HOGENOM; HOG000055453; -.
DR   OMA; DEPYDGI; -.
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: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;
DR   PRODOM; Q188Z4.
DR   SWISS-2DPAGE; Q188Z4.
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
//

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