ID A0A089M624_9BACL Unreviewed; 165 AA.
AC A0A089M624;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=R70331_12285 {ECO:0000313|EMBL:AIQ52204.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ52204.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ52204.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ52204.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009284; AIQ52204.1; -; Genomic_DNA.
DR RefSeq; WP_042175643.1; NZ_CP009284.1.
DR AlphaFoldDB; A0A089M624; -.
DR STRING; 1536773.R70331_12285; -.
DR KEGG; paee:R70331_12285; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_9; -.
DR Proteomes; UP000029487; Chromosome.
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; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000029487}.
FT DOMAIN 6..157
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 165 AA; 18946 MW; 741D124F380A6311 CRC64;
MKKFLKQWLP SIALGIVLSL FIRSYVAEAM RVPTDSMVPT IDVNDRLFVE KMLWMTKLKH
GDIVVFHPPV PGEEQKRYVK RLIGLPGDTV EIKDGALYRN GEQIAEPYLQ KPMDYTFGPV
TVPEEHYFFL GDNRNVSYDA HLWATPFVAK DQLVGKMLAN VNDMF
//