PRSW_OCEIH
ID PRSW_OCEIH Reviewed; 215 AA.
AC Q8EQA1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protease PrsW;
DE EC=3.4.-.-;
DE AltName: Full=Protease responsible for activating sigma-W;
GN Name=prsW; OrderedLocusNames=OB1807;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13763.1; -; Genomic_DNA.
DR RefSeq; WP_011066205.1; NC_004193.1.
DR AlphaFoldDB; Q8EQA1; -.
DR STRING; 221109.22777491; -.
DR MEROPS; M82.001; -.
DR EnsemblBacteria; BAC13763; BAC13763; BAC13763.
DR KEGG; oih:OB1807; -.
DR eggNOG; COG2339; Bacteria.
DR HOGENOM; CLU_081250_0_0_9; -.
DR OMA; DEPYDGI; -.
DR OrthoDB; 1626415at2; -.
DR PhylomeDB; Q8EQA1; -.
DR Proteomes; UP000000822; 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_0000248138"
FT TRANSMEM 1..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 215 AA; 24855 MW; 0AAC5451E15785A8 CRC64;
MLSILSAGIA PALALLSYIY LKDKITEPIW LIIRMFILGA LLVLPIMFIQ YAISSEFNYD
SIFIEAFFQI ALLEEFFKWF VFMFVIYQHE EFDNHYDGIV YASSLSLGFA SIENILYLIT
NGIEYAFLRA VFPVSSHALF GIIMGYYLGK AKTHTNYKKK NLTLAFLLPF LLHGIYNFIL
KGFSSFTLIL TPFMVLLWII ALYRLKRANE NTIIN