ID   RASP_GEOKA              Reviewed;         421 AA.
AC   Q5L0J5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=GK1256;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75541.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5L0J5; -.
DR   SMR; Q5L0J5; -.
DR   STRING; 235909.GK1256; -.
DR   MEROPS; M50.011; -.
DR   EnsemblBacteria; BAD75541; BAD75541; GK1256.
DR   KEGG; gka:GK1256; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000001172; 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..421
FT                   /note="Zinc metalloprotease RasP"
FT                   /id="PRO_0000248827"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          186..271
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        23
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"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   421 AA;  46681 MW;  972EA2C4E0A49C9E CRC64;
     MVETLESIIS FIVVFGALVF FHELGHLLLA KRAGILCREF AIGFGPKVFS FKKNETVYTI
     RLLPLGGFVR MAGEDPETIE LKRGQVVGLL LDESGQVEKI VLNHKDDYPN IRVVEVEEAD
     LEHGMYVTGY TDGERFERFT VKEPAFFVVD RQEIQIAPYH RQFAAKTLGQ RTMTILAGPL
     ANFLLSLVVF IIIGLLQGYP VDKPVIGELT PEGAARAAGL KQGDKVIAIN GERMETWTEI
     VNTIRAHPGE PLQFQIERNG KERSVTVTPE AKTVQGETIG LIGVYQPMEK SVLGSIKQGL
     VETYYWTREI VTGLGQLITG QFQLDMLSGP VGIAVSTGKV AESGIYYLMK WGAILSINLG
     IVNLLPLPAL DGGRLLFFAI EAVRGKPVDR QKEGMVHFIG FALLMLLMLV VTWNDIQKFF
     L