ID   LSPA_SALEP              Reviewed;         166 AA.
AC   B5R1N7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SEN0047;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
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DR   EMBL; AM933172; CAR31638.1; -; Genomic_DNA.
DR   RefSeq; WP_000042739.1; NC_011294.1.
DR   AlphaFoldDB; B5R1N7; -.
DR   SMR; B5R1N7; -.
DR   MEROPS; A08.001; -.
DR   KEGG; set:SEN0047; -.
DR   HOGENOM; CLU_083252_4_0_6; -.
DR   OMA; NRWYFPA; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000000613; 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 inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Protease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..166
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_1000097275"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   166 AA;  18339 MW;  CEDFB73FF9B924A0 CRC64;
     MSKPLCSTGL RWLWLVVVVL IIDLGSKYLI LQNFALGDTV GLFPSLNLHY ARNYGAAFSF
     LADSGGWQRW FFAGIAIGIC VILLVMMYRS KATQKLNNIA YALIIGGALG NLFDRLWHGF
     VVDMIDFYVG NWHFATFNLA DSAICIGAAL IVLEGFLPKP TAKEQA