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SEC11_LODEL
ID   SEC11_LODEL             Reviewed;         166 AA.
AC   A5DS09;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE            EC=3.4.21.89 {ECO:0000250|UniProtKB:P15367};
DE   AltName: Full=Signal peptidase I;
GN   Name=SEC11; ORFNames=LELG_00145;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDK41967.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CH981524; EDK41967.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001527625.1; XM_001527575.1.
DR   AlphaFoldDB; A5DS09; -.
DR   SMR; A5DS09; -.
DR   STRING; 379508.A5DS09; -.
DR   MEROPS; S26.010; -.
DR   EnsemblFungi; EDK41967; EDK41967; LELG_00145.
DR   GeneID; 5235618; -.
DR   KEGG; lel:LELG_00145; -.
DR   eggNOG; KOG3342; Eukaryota.
DR   HOGENOM; CLU_089996_0_2_1; -.
DR   InParanoid; A5DS09; -.
DR   OrthoDB; 1486616at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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   CDD; cd06530; S26_SPase_I; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR019533; Peptidase_S26.
DR   InterPro; IPR001733; Peptidase_S26B.
DR   PANTHER; PTHR10806; PTHR10806; 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; Hydrolase; Membrane; Protease; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..166
FT                   /note="Signal peptidase complex catalytic subunit SEC11"
FT                   /id="PRO_0000412335"
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..166
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          152..163
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        108
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
SQ   SEQUENCE   166 AA;  18843 MW;  7283AC3C1B491017 CRC64;
     MNIRQQLTQL LTLGYVFASA FMLWKTLSVV ANLHSPIVVV LSGSMEPAFQ RGDILFLWNR
     DEKQKVGDIV VYEIEGKTIP IVHRVLREHH NLEKQLLLTK GDNNAVDDLS LYAKKQSYLN
     RKNDLVGTVK GYLPFIGYVT ILISENQYFK FGLLGLLGLS SLFSNE
 
 
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