ID A0A177EJ41_9MICR Unreviewed; 241 AA.
AC A0A177EJ41;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=NEIG_00791 {ECO:0000313|EMBL:OAG31491.1};
OS Nematocida sp. ERTm5.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=1805481 {ECO:0000313|EMBL:OAG31491.1, ECO:0000313|Proteomes:UP000077089};
RN [1] {ECO:0000313|EMBL:OAG31491.1, ECO:0000313|Proteomes:UP000077089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERTm5 {ECO:0000313|EMBL:OAG31491.1,
RC ECO:0000313|Proteomes:UP000077089};
RA Reinke A.W., Balla K.M., Bennett E.J., Troemel E.R.;
RT "Identification of microsporidia host-exposed proteins reveals a repertoire
RT of large paralogous families and rapidly evolving proteins.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAG31491.1}.
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; LTDK01000160; OAG31491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177EJ41; -.
DR VEuPathDB; MicrosporidiaDB:NEIG_00791; -.
DR OrthoDB; 1114626at2759; -.
DR Proteomes; UP000077089; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362047};
KW Protease {ECO:0000256|RuleBase:RU362047};
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 34..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT TRANSMEM 167..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT REGION 216..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 27850 MW; 8439DADE1EB7C790 CRC64;
MRVGDILSHV PMSDVIFSKE DIAYYNKLGM RQTILQLLQA SYMICSAYMV WMLVAVICNT
KSPIVVVLSE SMYPGFDRGD ILLLAKMRSE YYAGDICVFQ LADEDIPIVH RVIDKLYSKT
PIAGCEATTK NPLANHFQYM TKGDNNRSND IFLYREKGLR YINSKHMGTV VYASFPLLGM
VTIWTGYWKW LKYVIIGILA IDVAFTRDNT IKIARLDEKE KKQESEEEEE KEKKKKKEKQ
E
//
