PRSW_ALKCK
ID PRSW_ALKCK Reviewed; 215 AA.
AC Q5WGV5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
DE AltName: Full=Protease responsible for activating sigma-W;
GN Name=prsW; OrderedLocusNames=ABC1865;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the degradation of specific anti-sigma factors.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protease PrsW family. {ECO:0000305}.
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DR EMBL; AP006627; BAD64400.1; -; Genomic_DNA.
DR RefSeq; WP_011246708.1; NC_006582.1.
DR AlphaFoldDB; Q5WGV5; -.
DR STRING; 66692.ABC1865; -.
DR EnsemblBacteria; BAD64400; BAD64400; ABC1865.
DR KEGG; bcl:ABC1865; -.
DR eggNOG; COG2339; Bacteria.
DR HOGENOM; CLU_081250_0_0_9; -.
DR OMA; DEPYDGI; -.
DR OrthoDB; 1626415at2; -.
DR Proteomes; UP000001168; 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 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..215
FT /note="Protease PrsW"
FT /id="PRO_0000248135"
FT TRANSMEM 1..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 215 AA; 24114 MW; 20E9C7797B26E750 CRC64;
MVSLVLAALA PAMALFSYVY LRDVYSKAKM FLVLRIFIIG ALLVVPILVI QFAFTEENVF
PHPAAKAFLL YGFLEEGLKW LMLFVFAYQH GQLQRPGDGI LFGVSVSLGF ATVENGLYMI
AYGLEAAIPR TVLPTTAHAV YGIVMGYYIG QAKYKEDHKK MFLLLGAILP ILLHGGYDFI
LSSFGHYVLY AMIPFMVILW LLAIWKLKKA SRFTV
