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SEC11_YEASL
ID   SEC11_YEASL             Reviewed;         167 AA.
AC   E7KQ01;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE            EC=3.4.21.89 {ECO:0000250|UniProtKB:P15367};
DE   AltName: Full=Secretory protein 11;
DE   AltName: Full=Signal peptidase I;
GN   Name=SEC11; ORFNames=QA23_2427;
OS   Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin QA23;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- FUNCTION: Catalytic component of the signal peptidase complex (SPC)
CC       which catalyzes the cleavage of N-terminal signal sequences from
CC       nascent proteins as they are translocated into the lumen of the
CC       endoplasmic reticulum (By similarity). Specifically cleaves N-terminal
CC       signal peptides that contain a hydrophobic alpha-helix (h-region)
CC       shorter than 18-20 amino acids (By similarity).
CC       {ECO:0000250|UniProtKB:P15367, ECO:0000250|UniProtKB:P67812}.
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         Evidence={ECO:0000250|UniProtKB:P15367};
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC       catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and
CC       SPC3 (By similarity). The complex induces a local thinning of the ER
CC       membrane which is used to measure the length of the signal peptide (SP)
CC       h-region of protein substrates. This ensures the selectivity of the
CC       complex towards h-regions shorter than 18-20 amino acids (By
CC       similarity). SPC associates with the translocon complex (By
CC       similarity). {ECO:0000250|UniProtKB:P15367,
CC       ECO:0000250|UniProtKB:P67812}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P15367}.
CC   -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC       activity. It may be accommodated as a transmembrane helix in the
CC       thinned membrane environment of the complex, similarly to the signal
CC       peptide in the complex substrates. {ECO:0000250|UniProtKB:P67812}.
CC   -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR   EMBL; ADVV01000048; EGA82330.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7KQ01; -.
DR   SMR; E7KQ01; -.
DR   MEROPS; S26.010; -.
DR   EnsemblFungi; EGA82330; EGA82330; QA23_2427.
DR   HOGENOM; CLU_089996_0_0_1; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR001733; Peptidase_S26B.
DR   InterPro; IPR027245; Sec11.
DR   PANTHER; PTHR10806; PTHR10806; 1.
DR   PANTHER; PTHR10806:SF6; PTHR10806:SF6; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00728; SIGNALPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..167
FT                   /note="Signal peptidase complex catalytic subunit SEC11"
FT                   /id="PRO_0000412358"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..167
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          153..164
FT                   /note="C-terminal short (CTS) helix"
FT                   /evidence="ECO:0000250|UniProtKB:P67812"
FT   ACT_SITE        44
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   ACT_SITE        83
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   167 AA;  18762 MW;  FC877232D6888DF3 CRC64;
     MNLRFELQKL LNVCFLFASA YMFWQGLAIA TNSASPIVVV LSGSMEPAFQ RGDILFLWNR
     NTFNQVGDVV VYEVEGKQIP IVHRVLRQHN NHADKQFLLT KGDNNAGNDI SLYANKKIYL
     NKSKEIVGTV KGYFPQLGYI TIWISENKYA KFALLGMLGL SALLGGE
 
 
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