SEC11_TUBMM
ID SEC11_TUBMM Reviewed; 186 AA.
AC D5GNC3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=GSTUM_00011219001;
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28;
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN430363; CAZ86016.1; -; Genomic_DNA.
DR RefSeq; XP_002841825.1; XM_002841779.1.
DR AlphaFoldDB; D5GNC3; -.
DR SMR; D5GNC3; -.
DR STRING; 656061.D5GNC3; -.
DR MEROPS; S26.010; -.
DR EnsemblFungi; CAZ86016; CAZ86016; GSTUM_00011219001.
DR GeneID; 9182216; -.
DR KEGG; tml:GSTUM_00011219001; -.
DR eggNOG; KOG3342; Eukaryota.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; D5GNC3; -.
DR OMA; YNVRGKD; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
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; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR PANTHER; PTHR10806; PTHR10806; 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..186
FT /note="Signal peptidase complex catalytic subunit SEC11"
FT /id="PRO_0000412369"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..186
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 172..183
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 55
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 102
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
SQ SEQUENCE 186 AA; 20817 MW; 0B0D4F19E875C8F6 CRC64;
MDALGLSKLR HLKPRQLLSQ VLNFALILST AFMLWKGLSV ATDSPSPIVV VLSGSMEPAF
QRGDLLFLWN RNLELDSPPT PGTRVGEIVV YNVIGKDIPI VHRVVRKHQG PKTPLHLLTK
GDNNHADDTE LYARGRWYLD REKEVIGSVV GYVPFVGYVT IMLSEHPWMK TALLGIMGLL
VIVQRE
