ID   LEP2_SYNY3              Reviewed;         218 AA.
AC   P73157;
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-2;
DE            Short=SPase I-2;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I-2;
GN   Name=lepB2; OrderedLocusNames=slr1377;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA17183.1; -; Genomic_DNA.
DR   PIR; S75269; S75269.
DR   AlphaFoldDB; P73157; -.
DR   SMR; P73157; -.
DR   STRING; 1148.1652260; -.
DR   MEROPS; S26.008; -.
DR   PaxDb; P73157; -.
DR   EnsemblBacteria; BAA17183; BAA17183; BAA17183.
DR   KEGG; syn:slr1377; -.
DR   eggNOG; COG0681; Bacteria.
DR   InParanoid; P73157; -.
DR   OMA; ACDAYIK; -.
DR   PhylomeDB; P73157; -.
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..218
FT                   /note="Probable signal peptidase I-2"
FT                   /id="PRO_0000109536"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..218
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  24733 MW;  F081C2AE157B20DD CRC64;
     MTENIVRETS KKKESPPENT WLELGKTMVT AVILAIGIRT FVAEARYIPS SSMEPTLQIN
     DRLIIEKISY RLRDPERGEI VVFNPTDALK AKNFHDAFIK RIIGLPGDEV RVSQGNVYVN
     GKMLDENYIA APPAYEYGPV KVPDDQYLVL GDNRNNSYDS HYWGFVPREK LLGRAFVRFW
     PVPRVGLLTD DAEREAVEIS PQAWESPAIS PQTVPESR