SEC11_LEPMJ
ID SEC11_LEPMJ Reviewed; 173 AA.
AC E5A8D2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 25-MAY-2022, entry version 52.
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=Lema_P074660;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(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; FP929137; CBX99877.1; -; Genomic_DNA.
DR RefSeq; XP_003843356.1; XM_003843308.1.
DR AlphaFoldDB; E5A8D2; -.
DR SMR; E5A8D2; -.
DR STRING; 985895.E5A8D2; -.
DR MEROPS; S26.010; -.
DR EnsemblFungi; CBX99877; CBX99877; LEMA_P074660.1.
DR GeneID; 13292699; -.
DR eggNOG; KOG3342; Eukaryota.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; E5A8D2; -.
DR OMA; YNVRGKD; -.
DR OrthoDB; 1486616at2759; -.
DR Proteomes; UP000002668; Genome.
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 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; 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..173
FT /note="Signal peptidase complex catalytic subunit SEC11"
FT /id="PRO_0000412334"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..173
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 159..170
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 50
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 89
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 173 AA; 19034 MW; 22B1154CD80641F7 CRC64;
MLGVSGMQPR QLAAQILNFA LVLSTAFMMW KGLSVVSDSS SPIVVVLSGS MEPAFQRGDL
LFLWNRGLDT QVGEIVVYNV KGKDIPIVHR VVRRYGGGKT PLRLLTKGDN NIADDTELYA
TSQSFLTRKE DVVGSVVGFI PFVGYVTILL SENPWMKQVM LGLMGVMVVL QRE
