ID L7JT39_TRAHO Unreviewed; 176 AA.
AC L7JT39;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000256|ARBA:ARBA00019685, ECO:0000256|RuleBase:RU362047};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362047};
GN ORFNames=THOM_2427 {ECO:0000313|EMBL:ELQ74643.1};
OS Trachipleistophora hominis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Trachipleistophora.
OX NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ74643.1, ECO:0000313|Proteomes:UP000011185};
RN [1] {ECO:0000313|EMBL:ELQ74643.1, ECO:0000313|Proteomes:UP000011185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA Embley T.M.;
RT "The genome of the obligate intracellular parasite Trachipleistophora
RT hominis: new insights into microsporidian genome dynamics and reductive
RT evolution.";
RL PLoS Pathog. 8:E1002979-E1002979(2012).
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. {ECO:0000256|ARBA:ARBA00029411}.
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:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU362047};
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.
CC {ECO:0000256|ARBA:ARBA00029478}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family.
CC {ECO:0000256|ARBA:ARBA00011035, ECO:0000256|RuleBase:RU362047}.
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DR EMBL; JH994033; ELQ74643.1; -; Genomic_DNA.
DR AlphaFoldDB; L7JT39; -.
DR STRING; 72359.L7JT39; -.
DR MEROPS; S26.010; -.
DR VEuPathDB; MicrosporidiaDB:THOM_2427; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; L7JT39; -.
DR OMA; IPVVWFP; -.
DR Proteomes; UP000011185; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR PANTHER; PTHR10806:SF6; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362047};
KW Hydrolase {ECO:0000256|RuleBase:RU362047, ECO:0000313|EMBL:ELQ74643.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362047};
KW Protease {ECO:0000256|RuleBase:RU362047};
KW Reference proteome {ECO:0000313|Proteomes:UP000011185};
KW Signal-anchor {ECO:0000256|RuleBase:RU362047};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362047};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362047}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT TRANSMEM 148..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
SQ SEQUENCE 176 AA; 20523 MW; 3DD939C263024A22 CRC64;
MFDLFFSPKE IRNLKRMSKR QLLLQFVNAS YSVMGTYMLW KLIGLFLNND SPIVVVLSES
MEPGFKRGDI LFLSPRSYDV GDMTVFQINK KEIPIVHRAI RKLGTKVLTK GDNNLRDDVP
LYRPGQYMLE PNDILSCVFG YIPYFGMITI WINTFPWIKV LILFCIGMTV FFTRDE
//
