ID   LSPA_STRGG              Reviewed;         196 AA.
AC   B1W0K0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE            EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161};
DE            Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161};
GN   Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161}; OrderedLocusNames=SGR_5431;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC       peptides from prolipoproteins. {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of signal peptides from bacterial membrane
CC         prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in
CC         which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and
CC         Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00161};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC       cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00161};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
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DR   EMBL; AP009493; BAG22260.1; -; Genomic_DNA.
DR   RefSeq; WP_003969717.1; NC_010572.1.
DR   AlphaFoldDB; B1W0K0; -.
DR   SMR; B1W0K0; -.
DR   STRING; 455632.SGR_5431; -.
DR   EnsemblBacteria; BAG22260; BAG22260; SGR_5431.
DR   GeneID; 6211856; -.
DR   KEGG; sgr:SGR_5431; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_2_2_11; -.
DR   OMA; PKHFAVF; -.
DR   OrthoDB; 1575081at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001685; Chromosome.
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:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695; PTHR33695; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   TIGRFAMs; TIGR00077; lspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cell membrane; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..196
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_1000097283"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   196 AA;  20563 MW;  A2672B7D7B769EA6 CRC64;
     MAEAERIIGM PENPDVDGTD EGGSTAADAA VNAGRGKRKI LALLSVAVVA YLLDLGSKML
     VVAKLEHQPP IDIIGDWLQF RAIRNPGAAF GIGEAFTVIF TIIATGVIVV IFRIARKLYS
     LPWAIALGLL LGGALGNLTD RIFRAPGVFE GAVVDFIAPK NSAVFNLADS AIVCGGILIV
     ILSFKGLDPD GTVHKD