RSEP_ECO57
ID RSEP_ECO57 Reviewed; 450 AA.
AC P0AEH2; P37764;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=Z0187, ECs0178;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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; AE005174; AAG54478.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33601.1; -; Genomic_DNA.
DR PIR; B85502; B85502.
DR PIR; B90651; B90651.
DR RefSeq; NP_308205.1; NC_002695.1.
DR RefSeq; WP_001295561.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEH2; -.
DR SMR; P0AEH2; -.
DR STRING; 155864.EDL933_0181; -.
DR MEROPS; M50.004; -.
DR PRIDE; P0AEH2; -.
DR EnsemblBacteria; AAG54478; AAG54478; Z0187.
DR EnsemblBacteria; BAB33601; BAB33601; ECs_0178.
DR GeneID; 66671536; -.
DR GeneID; 913885; -.
DR KEGG; ece:Z0187; -.
DR KEGG; ecs:ECs_0178; -.
DR PATRIC; fig|386585.9.peg.281; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_2_6; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000088418"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
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; 49071 MW; 81A93BC113FBB66C CRC64;
MLSFLWDLAS FIVALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RTDKLGTEYV
IALIPLGGYV KMLDERAEPV VPELRHHAFN NKSVGQRAAI IAAGPVANFI FAIFAYWLVF
IIGVPGVRPV VGEIAANSIA AEAQIAPGTE LKAVDGIETP DWDAVRLQLV DKIGDESTTI
TVAPFGSDQR RDVKLDLRHW AFEPDKEDPV SSLGIRPRGP QIEPVLENVQ PNSAASKAGL
QAGDRIVKVD GQPLTQWVTF VMLVRDNPGK SLALEIERQG SPLSLTLIPE SKPGNGKAIG
FVGIEPKVIP LPDEYKVVRQ YGPFNAIVEA TDKTWQLMKL TVSMLGKLIT GDVKLNNLSG
PISIAKGAGM TAELGVVYYL PFLALISVNL GIINLFPLPV LDGGHLLFLA IEKIKGGPVS
ERVQDFCYRI GSILLVLLMG LALFNDFSRL
