(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 88.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the
CC       transmembrane region of RseA. Part of a regulated intramembrane
CC       proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release
CC       the cytoplasmic domain of RseA. This provides the cell with sigma-
CC       E (RpoE) activity through the proteolysis of RseA (By similarity).
CC       {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-
CC       pass 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
CC       when an extracytoplasmic signal triggers a concerted proteolytic
CC       cascade to transmit information and elicit cellular responses. A
CC       membrane-spanning regulatory substrate protein is first cut
CC       extracytoplasmically (site-1 protease, S1P), then within the
CC       membrane itself (site-2 protease, S2P, this enzyme), while
CC       cytoplasmic proteases finish degrading the regulatory protein,
CC       liberating the effector protein (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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_MWVM01000012.1.
DR   ProteinModelPortal; P0AEH2; -.
DR   SMR; P0AEH2; -.
DR   STRING; 155864.Z0187; -.
DR   EnsemblBacteria; AAG54478; AAG54478; Z0187.
DR   EnsemblBacteria; BAB33601; BAB33601; BAB33601.
DR   GeneID; 913885; -.
DR   KEGG; ece:Z0187; -.
DR   KEGG; ecs:ECs0178; -.
DR   PATRIC; fig|386585.9.peg.281; -.
DR   eggNOG; ENOG4105DZP; Bacteria.
DR   eggNOG; COG0750; LUCA.
DR   HOGENOM; HOG000006281; -.
DR   KO; K11749; -.
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   InterPro; IPR001478; PDZ.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   Pfam; PF00595; PDZ; 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;
DR   PRODOM; P0AEH2.
DR   SWISS-2DPAGE; P0AEH2.
KW   Cell inner membrane; Cell membrane; Complete proteome; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Protease; Repeat;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN         1    450       Regulator of sigma E protease.
FT                                /FTId=PRO_0000088418.
FT   TRANSMEM    107    127       Helical. {ECO:0000255}.
FT   TRANSMEM    376    396       Helical. {ECO:0000255}.
FT   TRANSMEM    430    450       Helical. {ECO:0000255}.
FT   DOMAIN      115    186       PDZ 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      199    291       PDZ 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   ACT_SITE     23     23       {ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL        22     22       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL        26     26       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                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
//

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