(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 103.
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}.
DR   EMBL; AE006468; AAL19187.1; -; Genomic_DNA.
DR   RefSeq; NP_459228.1; NC_003197.2.
DR   RefSeq; WP_000949017.1; NC_003197.2.
DR   SMR; Q8ZRP1; -.
DR   MEROPS; M50.004; -.
DR   PaxDb; Q8ZRP1; -.
DR   PRIDE; Q8ZRP1; -.
DR   EnsemblBacteria; AAL19187; AAL19187; STM0223.
DR   GeneID; 1251741; -.
DR   KEGG; stm:STM0223; -.
DR   PATRIC; fig|99287.12.peg.236; -.
DR   eggNOG; ENOG4105DZP; Bacteria.
DR   eggNOG; COG0750; LUCA.
DR   HOGENOM; HOG000006281; -.
DR   KO; K11749; -.
DR   OMA; QYMVGFG; -.
DR   PhylomeDB; Q8ZRP1; -.
DR   BioCyc; SENT99287:STM0223-MONOMER; -.
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   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   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;
DR   PRODOM; Q8ZRP1.
DR   SWISS-2DPAGE; Q8ZRP1.
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   METAL           22
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           26
FT                   /note="Zinc; 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
//

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