ID   LEP1_SYNY3              Reviewed;         196 AA.
AC   P72660;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=Probable signal peptidase I-1;
DE            Short=SPase I-1;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I-1;
GN   Name=lepB1; OrderedLocusNames=sll0716;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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 membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA16662.1; -; Genomic_DNA.
DR   PIR; S74510; S74510.
DR   AlphaFoldDB; P72660; -.
DR   SMR; P72660; -.
DR   IntAct; P72660; 3.
DR   STRING; 1148.1651734; -.
DR   MEROPS; S26.008; -.
DR   PaxDb; P72660; -.
DR   EnsemblBacteria; BAA16662; BAA16662; BAA16662.
DR   KEGG; syn:sll0716; -.
DR   eggNOG; COG0681; Bacteria.
DR   InParanoid; P72660; -.
DR   OMA; IEPRWIP; -.
DR   PhylomeDB; P72660; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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 membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..196
FT                   /note="Probable signal peptidase I-1"
FT                   /id="PRO_0000109535"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..196
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   196 AA;  22230 MW;  EB02533BF7341573 CRC64;
     MQNSPIPSPW QFIKENIPLL MVALVLALLL RFFVAEPRYI PSDSMLPTLE QGDRLVVEKV
     SYHFHPPQVG DIIVFHPPEL LQVQGYDLGQ AFIKRVIALP GQTVEVNNGI VYRDGQPLQE
     EYILEPPQYN LPAVRVPDGQ VFVMGDNRNN SNDSHVWGFL PQQNIIGHAL FRFFPASRWG
     QLGSFTFVPA RTIINT