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LEP_SALTY
ID   LEP_SALTY               Reviewed;         324 AA.
AC   P0A1W2; P23697;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Signal peptidase I;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=lepB; OrderedLocusNames=STM2582;
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 [GENOMIC DNA].
RC   STRAIN=PP1139;
RX   PubMed=2250650; DOI=10.1007/bf00265059;
RA   van Dijl J.M., van den Bergh R., Reversma T., Smith H., Bron S., Venema G.;
RT   "Molecular cloning of the Salmonella typhimurium lep gene in Escherichia
RT   coli.";
RL   Mol. Gen. Genet. 223:233-240(1990).
RN   [2]
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; X54933; CAA38694.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21476.1; -; Genomic_DNA.
DR   PIR; S12020; S12020.
DR   RefSeq; NP_461517.1; NC_003197.2.
DR   RefSeq; WP_000002559.1; NC_003197.2.
DR   AlphaFoldDB; P0A1W2; -.
DR   SMR; P0A1W2; -.
DR   STRING; 99287.STM2582; -.
DR   MEROPS; S26.001; -.
DR   PaxDb; P0A1W2; -.
DR   EnsemblBacteria; AAL21476; AAL21476; STM2582.
DR   GeneID; 1254104; -.
DR   KEGG; stm:STM2582; -.
DR   PATRIC; fig|99287.12.peg.2723; -.
DR   HOGENOM; CLU_028723_1_1_6; -.
DR   OMA; SDSRFWG; -.
DR   PhylomeDB; P0A1W2; -.
DR   BioCyc; SENT99287:STM2582-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.170.230.10; -; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   InterPro; IPR019766; Sign_pep_all-beta_subdom.
DR   PANTHER; PTHR43390; PTHR43390; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 2.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..324
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109518"
FT   TOPO_DOM        1..3
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..324
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35778 MW;  40607CDA15779575 CRC64;
     MANMFALILV IATLVTGILW CVDKFVFAPK RRARQAAAQT ASGDALDNAT LNKVAPKPGW
     LETGASVFPV LAIVLIVRSF LYEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPIYQKTL
     IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKITYDP VAKEVTIQPG CSSGQACENA
     LPVTYSNVEP SDFVQTFARR NGGEATSGFF EVPLNETKEN GIRLTERKET LGDVTHRILM
     VPIAQDQLGM YYQQPGQPLA TWVVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGKAVAI
     WMSFDKQEGE WPTGVRLSRI GGIH
 
 
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