ID   RSEP_PHOLU              Reviewed;         226 AA.
AC   Q9S342;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protease RseP;
DE            EC=3.4.24.-;
DE   AltName: Full=S2P endopeptidase;
DE   AltName: Full=Site-2 protease RseP;
DE            Short=S2P protease RseP;
DE   AltName: Full=Site-2-type intramembrane protease;
DE   Flags: Fragment;
GN   Name=rseP;
OS   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hm;
RA   Chatonnet-Marton P.I., Givaudan A., Lanois A., Boemare N.E.;
RT   "Photorhabdus luminescens genomic region homologous to 4.0 minute
RT   Escherichia coli region promotes pleiotropic phenotypes.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves
CC       the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane
CC       region of RseA. Part of a regulated intramembrane proteolysis (RIP)
CC       cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of
CC       RseA. This provides the cell with sigma-E (RpoE) activity through the
CC       proteolysis of RseA (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with RseA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The 2 circularly premutated PDZ domains act to negatively
CC       regulate protease action on intact RseA. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs when an
CC       extracytoplasmic signal triggers a concerted proteolytic cascade to
CC       transmit information and elicit cellular responses. A membrane-spanning
CC       regulatory substrate protein is first cut extracytoplasmically (site-1
CC       protease, S1P), then within the membrane itself (site-2 protease, S2P,
CC       this enzyme), while cytoplasmic proteases finish degrading the
CC       regulatory protein, liberating the effector protein (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AJ236920; CAB51928.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S342; -.
DR   SMR; Q9S342; -.
DR   STRING; 29488.KS18_15810; -.
DR   MEROPS; M50.004; -.
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: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; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metalloprotease;
KW   Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           <1..226
FT                   /note="Protease RseP"
FT                   /id="PRO_0000088419"
FT   TRANSMEM        152..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..56
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   NON_TER         1
SQ   SEQUENCE   226 AA;  24535 MW;  B7955D5AF2839D43 CRC64;
     VEKVIPGSAA EKAGLQKGDR IVKVGSQEID VWHTFTSFVS NNPNVPLELS VDRAGHIISL
     SMTPEVRQQS GGRKVGFAGV ELRIVPLADE YKIVQQYGPF SAMYQAGDKT WQLMRLTVSM
     IGKLIVGDVK INNLSGPISI AKGAGVSADS GLVYYLMFLA LISVNLGIIN LIPLPVLDGG
     HLLFLFIEKI KGGPVSERVQ DFSYRIGAMI LVLLMGLALF NDFSRF