ID   LSPA_STRMU              Reviewed;         153 AA.
AC   Q8DUQ0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=SMU_853;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58569.1; -; Genomic_DNA.
DR   RefSeq; NP_721263.1; NC_004350.2.
DR   RefSeq; WP_002262002.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUQ0; -.
DR   SMR; Q8DUQ0; -.
DR   STRING; 210007.SMU_853; -.
DR   EnsemblBacteria; AAN58569; AAN58569; SMU_853.
DR   KEGG; smu:SMU_853; -.
DR   PATRIC; fig|210007.7.peg.759; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_3_3_9; -.
DR   OMA; NRWYFPA; -.
DR   PhylomeDB; Q8DUQ0; -.
DR   BRENDA; 3.4.23.36; 5941.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000002512; 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   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..153
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_0000289438"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   153 AA;  17340 MW;  4208C178E9CBBE4A CRC64;
     MRKIVLAVTA LLLVALDQLS KFFVVKYIRL GTIVEFIPNL VSLTYLRNTG AAFSILENQQ
     WLFTVITFIV LGVAFYYLIK QMQTQNFWLL ASLLLIISGG LGNFIDRLRL GYVVDMIHLD
     FVDFAIFNVA DSYLSVGVAL LIIALWKEEK NGN