ID N2AI49_9FIRM Unreviewed; 209 AA.
AC N2AI49;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=C823_03342 {ECO:0000313|EMBL:EMZ24079.1};
OS Eubacterium plexicaudatum ASF492.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ24079.1, ECO:0000313|Proteomes:UP000012589};
RN [1] {ECO:0000313|EMBL:EMZ24079.1, ECO:0000313|Proteomes:UP000012589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF492 {ECO:0000313|EMBL:EMZ24079.1,
RC ECO:0000313|Proteomes:UP000012589};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
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:RU362042};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606,
CC ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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:EMZ24079.1}.
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DR EMBL; AQFT01000100; EMZ24079.1; -; Genomic_DNA.
DR RefSeq; WP_004064894.1; NZ_AQFT02000001.1.
DR AlphaFoldDB; N2AI49; -.
DR STRING; 1235802.C823_03342; -.
DR GeneID; 78437164; -.
DR PATRIC; fig|1235802.3.peg.3527; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_9; -.
DR Proteomes; UP000012589; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000012589};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 24..199
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 209 AA; 24601 MW; 1B09CC29462495B4 CRC64;
MAKNAKSEKT EMEEQKRPWW KELLSYVWII LFACVAAMAV NRYVLINAEI PSESMENLLT
VDDRIFGCRL SYVFGEPERY DVVMFRYPVH EDTIYIKRII GLPGETVEIR KGKIYIDGSE
TPIEEDYLPE KWTDGNDGYL FEVPKDSYLM LGDNRNLSED ARYWAQCALD DEVASNKEEA
QKYTYVREDQ MIGRAILKYY PKFHLFLNI
//
