PRSW_GEOKA
ID PRSW_GEOKA Reviewed; 225 AA.
AC Q5KXR9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
DE AltName: Full=Protease responsible for activating sigma-W;
GN Name=prsW; OrderedLocusNames=GK2232;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD76517.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000043; BAD76517.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012820744.1; NC_006510.1.
DR AlphaFoldDB; Q5KXR9; -.
DR STRING; 235909.GK2232; -.
DR MEROPS; M82.001; -.
DR EnsemblBacteria; BAD76517; BAD76517; GK2232.
DR KEGG; gka:GK2232; -.
DR eggNOG; COG2339; Bacteria.
DR HOGENOM; CLU_081250_0_0_9; -.
DR Proteomes; UP000001172; 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..225
FT /note="Protease PrsW"
FT /id="PRO_0000248137"
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..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 225 AA; 25541 MW; 1A070F9D3E68724E CRC64;
MFSLISAGVA PGVALLSYFY LKDEYEAEPL SFVLRMFLFG VLLVFPIMFI QYVLAAEGIV
ASPAAEAFLS AALLEEFVKW FVVYFFVYDH DEFDEPYDGI VYSASVSLGF ATLENILYLL
ANGVETAIAR ALLPVSSHAL FSVIMGFYFG KAKFAVKKRR YYLWASFLLP FFLHGVYDWL
LLAKERWGYY MGLFMLALWW AALRKVKQAK GYARPQAVPP VKSQA