ID   RASP_ALKCK              Reviewed;         418 AA.
AC   Q5WFT5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Zinc metalloprotease RasP;
DE            EC=3.4.24.-;
DE   AltName: Full=Regulating alternative sigma factor protease;
DE   AltName: Full=Regulating anti-sigma-W factor activity protease;
GN   Name=rasP; OrderedLocusNames=ABC2235;
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: Is responsible for Site-2 cleavage of the RsiW anti-sigma
CC       factor. This results, after a third proteolytic step catalyzed by the
CC       ClpXP protease, in the release of SigW and the transcription activation
CC       of the genes under the control of the sigma-W factor (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AP006627; BAD64770.1; -; Genomic_DNA.
DR   RefSeq; WP_011247078.1; NC_006582.1.
DR   AlphaFoldDB; Q5WFT5; -.
DR   SMR; Q5WFT5; -.
DR   STRING; 66692.ABC2235; -.
DR   EnsemblBacteria; BAD64770; BAD64770; ABC2235.
DR   KEGG; bcl:ABC2235; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..418
FT                   /note="Zinc metalloprotease RasP"
FT                   /id="PRO_0000248825"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          183..267
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   418 AA;  46057 MW;  3D3C950607267A14 CRC64;
     MNTLLAFIAI FSVLVFVHEW GHLYFAKKAG ILCYEFAIGM GPKLFAFERN DTIYTIRLLP
     IGGYVRMAGE EPEQPTIRPG YEIGLVLDEK DTVKELIVNN KSKHPEAQVV QVERIDLVHD
     LFVETIDEDT GELVRYPIDE KAFIVQDEVA QIIAPWKRQF GSKPLPKRAM AIFAGPLMNF
     ILGFVILLGL SLYQGVTLSS EIVINGENSP AEAAGLQDGD VITAVNGVEV DSWKEMTTEV
     KKYPGEEVSI DYERNGEALQ TNATLSQVEV MPDEYEGFLG VSGVPEFSLL GSLQYAGNEF
     INMATSIFDT LGLIFTGQFS LDYISGPVGI YDITDQAVSL GIQTVIFFAA LLSINLGVIN
     LMPIPALDGG RLMFLAYEGI RGKPVSPEKE GAIQFIGFAL VMLLMIVVTW NDISKLFS