PRSW_ALKHC
ID PRSW_ALKHC Reviewed; 215 AA.
AC Q9KCE6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
DE AltName: Full=Protease responsible for activating sigma-W;
GN Name=prsW; OrderedLocusNames=BH1625;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05344.1; -; Genomic_DNA.
DR PIR; A83853; A83853.
DR RefSeq; WP_010897788.1; NC_002570.2.
DR AlphaFoldDB; Q9KCE6; -.
DR STRING; 272558.10174242; -.
DR EnsemblBacteria; BAB05344; BAB05344; BAB05344.
DR KEGG; bha:BH1625; -.
DR eggNOG; COG2339; Bacteria.
DR HOGENOM; CLU_081250_0_0_9; -.
DR OMA; DEPYDGI; -.
DR OrthoDB; 1626415at2; -.
DR Proteomes; UP000001258; 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_0000248134"
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; 24818 MW; 3959DB00BFE55CF6 CRC64;
MFSLLTAAIA PAMALLCFFY LKNEYGSQTL GFVVRTFLIG ALLMFPVMVL QHAFLAEGFF
ANPLLKAFIL YGFFEEFFKW FMLYFFAYKH VEFNRRYDGI IFGVSLSLGF ASMENGLYLI
ANGVETALGR ALLPVSSHAI YGVIMGYYLG RAKMEEKHRK KWLVLSLFLP VLLHSLYDAI
LLLWSKHFLF VMVPFMLVLW WVAIQKVKLA NQLDR