ID   RASP_ALKHC              Reviewed;         420 AA.
AC   Q9KA70;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=BH2420;
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: 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; BA000004; BAB06139.1; -; Genomic_DNA.
DR   PIR; D83952; D83952.
DR   RefSeq; WP_010898573.1; NC_002570.2.
DR   AlphaFoldDB; Q9KA70; -.
DR   SMR; Q9KA70; -.
DR   STRING; 272558.10175040; -.
DR   MEROPS; M50.011; -.
DR   EnsemblBacteria; BAB06139; BAB06139; BAB06139.
DR   KEGG; bha:BH2420; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
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: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; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
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..420
FT                   /note="Zinc metalloprotease RasP"
FT                   /id="PRO_0000088428"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          182..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   420 AA;  46476 MW;  2B6ADA6F6B0C1003 CRC64;
     MQTLIAFLVM FGVLVSVHEW GHLYFAKRAG ILCREFAIGF GPKLFSWKRN ETVYTIRLIP
     LGGYVRMAGE DPELITIKPG YEVGLVFNEK NVVSRIIVNN KSKHPEAQVV QVERIDLERE
     LFIEAYDDDG ERKRWDVDPK AEMVQDEEAT QIAPYDRQFG SKSVAQRALA IFAGPLMNFV
     LAFVLLAAYG FMQGIPVEDP VVGNIAENSA AETAGLQKGD YVLSIDGQTL ETWVDMTMII
     QQHPNEEITF EVERAGQILQ IPVTPNQVEG MDGEPIGLVG IERPAPEPAT LVSGLQFGAT
     QTYTYMTMIF DVLRLLVTGQ FSLDYVAGPV GIVNYTGQAA EMGIFVLLQW TAALSVNLGI
     VNLLPLPALD GGRLVFLGLE AVRGKPLDPS KESLVHFVGF ALLMLLVLVV TWNDINRLFL