SEC11_SCLS1
ID SEC11_SCLS1 Reviewed; 172 AA.
AC A7E716;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=SS1G_01092;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(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; CH476622; EDN96168.1; -; Genomic_DNA.
DR RefSeq; XP_001596900.1; XM_001596850.1.
DR AlphaFoldDB; A7E716; -.
DR SMR; A7E716; -.
DR STRING; 665079.A7E716; -.
DR MEROPS; S26.010; -.
DR EnsemblFungi; EDN96168; EDN96168; SS1G_01092.
DR GeneID; 5493698; -.
DR KEGG; ssl:SS1G_01092; -.
DR eggNOG; KOG3342; Eukaryota.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; A7E716; -.
DR OMA; YNVRGKD; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..172
FT /note="Signal peptidase complex catalytic subunit sec11"
FT /id="PRO_0000412365"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..172
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 158..169
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 49
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 115
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
SQ SEQUENCE 172 AA; 19107 MW; B78E532157EB8A65 CRC64;
MLSFLQNPRQ AAAQVLNFAL ILSTAFMMWK GLSVASDSPS PIVVVLSGSM EPAFQRGDLL
FLWNRNLLEE TKVGEIVVYN VKGKDIPIVH RLVRKFGAGP KAKLLTKGDN NVADDTELYA
RGQDYIERED IIGSVVGYIP FVGYVTILLS EHPWLKTVML GMMGLVVVLQ RE
