ID   LEP_PSEFL               Reviewed;         284 AA.
AC   P26844;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Signal peptidase I;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=lepB;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49323 / NCIMB 10586;
RX   PubMed=1546969; DOI=10.1042/bj2820539;
RA   Black M.T., Munn J.G.R., Allsop A.E.;
RT   "On the catalytic mechanism of prokaryotic leader peptidase 1.";
RL   Biochem. J. 282:539-543(1992).
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   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; X56466; CAA39839.1; -; Genomic_DNA.
DR   PIR; S22414; S22414.
DR   AlphaFoldDB; P26844; -.
DR   SMR; P26844; -.
DR   STRING; 690597.JH730941_gene3341; -.
DR   MEROPS; S26.001; -.
DR   eggNOG; COG0681; Bacteria.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   PANTHER; PTHR43390; PTHR43390; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..284
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109514"
FT   TRANSMEM        4..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..284
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  31903 MW;  B1B89D956BDA7891 CRC64;
     MSLNFPLLLV IAVAVCGLLA LLDLVFFAPR RRSAIASYQG SVSQPDAVVI EKLNKEPLLV
     EYGKSFFPVL FIVLVLRSFL VEPFQIPSGS MKPTLDVGDF ILVNKFSYGI RLPVIDKKVI
     EVGDPQRGDV MVFRYPSDPN VNYIKRVVGL PGDVVRYTSD KRLFINGESV AEKLLGAEPN
     TLGSAELYQE KLGAVEHEIR KEMSRYRAMP DGQWKVPAGH YFMMGDNRDN SNDSRYWDDP
     NIPKDLLGMV PDENIVGKAF AVWMSWPEPK LSHLPNFSRV GLIK