RSEP_SALTY
ID RSEP_SALTY Reviewed; 450 AA.
AC Q8ZRP1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Regulator of sigma E protease;
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;
GN Name=rseP; OrderedLocusNames=STM0223;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL19187.1; -; Genomic_DNA.
DR RefSeq; NP_459228.1; NC_003197.2.
DR RefSeq; WP_000949017.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRP1; -.
DR SMR; Q8ZRP1; -.
DR STRING; 99287.STM0223; -.
DR MEROPS; M50.004; -.
DR PaxDb; Q8ZRP1; -.
DR EnsemblBacteria; AAL19187; AAL19187; STM0223.
DR GeneID; 1251741; -.
DR KEGG; stm:STM0223; -.
DR PATRIC; fig|99287.12.peg.236; -.
DR HOGENOM; CLU_025778_0_2_6; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; Q8ZRP1; -.
DR BioCyc; SENT99287:STM0223-MON; -.
DR Proteomes; UP000001014; 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; -; 2.
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; 2.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..450
FT /note="Regulator of sigma E protease"
FT /id="PRO_0000088421"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 115..186
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 199..291
FT /note="PDZ 2"
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 450 AA; 49184 MW; 50A748A774A70B7B CRC64;
MLSILWNLAA FIIALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RTDRYGTEYV
IALIPLGGYV KMLDERAEPV APELRRHAFN NKTVGQRAAI IAAGPVANFI FAIFAYWLVF
IIGVPGVRPV IGEITPNSIA AQAQIAPGTE LKAVDGIETP DWDAVRLQLV SKIGDQQTTV
SVAPFGSDQR QDKTLDLRHW AFEPDKQDPV SSLGIRPRGP QIEPVLSEVQ ANSAASKAGL
QAGDRIVKVD GQPLTQWMKF VTFVRDNPGK PLALEIERQG SALSLTLTPD TKSVNGKAEG
FAGVVPKIIP LPEEYKTIRQ YGPFSAILEA TDKTWQLMKL TVSMLGKLIT GDVKLNNLSG
PISIAQGAGM SAEFGVIYYL MFLALISVNL GIINLFPLPV LDGGHLLFLA IEKLKGGPVS
ERVQDFSYRI GSILLVLLMG LALFNDFSRL
