ID A0A0V8QHR3_9FIRM Unreviewed; 162 AA.
AC A0A0V8QHR3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ASU35_07435 {ECO:0000313|EMBL:KSV59962.1};
OS Acetivibrio ethanolgignens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV59962.1, ECO:0000313|Proteomes:UP000054874};
RN [1] {ECO:0000313|EMBL:KSV59962.1, ECO:0000313|Proteomes:UP000054874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV59962.1,
RC ECO:0000313|Proteomes:UP000054874};
RA Zou Y., Xue W., Luo G., Lv M.;
RT "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing
RT bacterium of the family Lachnospiraceae isolated from the human faeces.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KSV59962.1}.
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DR EMBL; LNAM01000068; KSV59962.1; -; Genomic_DNA.
DR RefSeq; WP_058351854.1; NZ_LNAM01000068.1.
DR AlphaFoldDB; A0A0V8QHR3; -.
DR STRING; 290052.ASU35_07435; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000054874; 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; IPR019758; Pept_S26A_signal_pept_1_CS.
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; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000054874}.
FT DOMAIN 16..161
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 162 AA; 18676 MW; 8ADBC9C34BEF1834 CRC64;
MKLMKNYLKK ASLILAVFFF IYGVASFLND YLLQAEKIQG TSMEPLLTDG EMVFVSDIPF
WFSKPKRFDV IAFKKENTLY VKRIVGLPGE KIAVKNGNIY IDGQVVPENF GKEPISEDME
EMVLRKEEYF VLGDNRNFSI DSRSREIGAV KKEQIRGKVL FK
//
