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SEC11_KLULA
ID   SEC11_KLULA             Reviewed;         169 AA.
AC   Q6CMR5;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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; OrderedLocusNames=KLLA0E18261g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382125; CAG99861.1; -; Genomic_DNA.
DR   RefSeq; XP_454774.1; XM_454774.1.
DR   AlphaFoldDB; Q6CMR5; -.
DR   SMR; Q6CMR5; -.
DR   STRING; 28985.XP_454774.1; -.
DR   MEROPS; S26.010; -.
DR   EnsemblFungi; CAG99861; CAG99861; KLLA0_E18261g.
DR   GeneID; 2894751; -.
DR   KEGG; kla:KLLA0_E18261g; -.
DR   eggNOG; KOG3342; Eukaryota.
DR   HOGENOM; CLU_089996_0_0_1; -.
DR   InParanoid; Q6CMR5; -.
DR   OMA; YNVRGKD; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005787; C:signal peptidase complex; IEA:EnsemblFungi.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045047; P:protein targeting to ER; IEA:EnsemblFungi.
DR   GO; GO:0006465; P:signal peptide processing; IEA:EnsemblFungi.
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   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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..169
FT                   /note="Signal peptidase complex catalytic subunit SEC11"
FT                   /id="PRO_0000412331"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..169
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          154..165
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        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   169 AA;  18987 MW;  05B79B7FD21A2C9D CRC64;
     MNLRLELTRF LSLGYVLSSS FMFWMGLSLF TDCHSPIVVV LSGSMEPAFQ RGDILFLWNR
     NEKNNVGDVV VYEVAGKSIP IVHRVLKQHY DRSTGEQLLL TKGDNNNGDD VPLYARGNYY
     LNKTKDVVGT VKGYIPQLGY VTIWISENKY AKFGLLGLLA LSSLISSED
 
 
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