PRSW_BACLD
ID PRSW_BACLD Reviewed; 222 AA.
AC Q65I04; Q62TF2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
DE AltName: Full=Protease responsible for activating sigma-W;
GN Name=prsW; OrderedLocusNames=BLi02432, BL02223;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [3]
RP SEQUENCE REVISION.
RA Berka R.M., Rey M.W., Ramaiya P.;
RL Submitted (APR-2007) 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; AE017333; AAU41310.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU23957.2; -; Genomic_DNA.
DR RefSeq; WP_003183040.1; NC_006322.1.
DR AlphaFoldDB; Q65I04; -.
DR STRING; 279010.BL02223; -.
DR MEROPS; M82.001; -.
DR EnsemblBacteria; AAU23957; AAU23957; BL02223.
DR GeneID; 66215568; -.
DR KEGG; bld:BLi02432; -.
DR KEGG; bli:BL02223; -.
DR eggNOG; COG2339; Bacteria.
DR HOGENOM; CLU_081250_0_0_9; -.
DR OMA; DEPYDGI; -.
DR OrthoDB; 1626415at2; -.
DR BioCyc; BLIC279010:BLI_RS12060-MON; -.
DR Proteomes; UP000000606; 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..222
FT /note="Protease PrsW"
FT /id="PRO_0000248136"
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..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 222 AA; 25527 MW; 20D44029E6B91166 CRC64;
MFGIISAGLA PGIALLMYFY LKEKYESEPI HMVIRLFILG VLLVFPTMFI QYVLEKEHIS
EGSFVVSFLT SGFLEEFLKW FLLMVSTFQH IDFDEHYDGI VYGTSLSLGF ATLENILYLI
GNGVEYAFMR ALLPVSSHAL FGVIMGFYIG KARFSDSKTK MKWLLCSLFI PALLHGLYDY
ILLALKNWIY FMLPFMAFLW WFGLRKAKKA RSVKTGGQPL QQ
