ID   LSPA_SYNWW              Reviewed;         149 AA.
AC   Q0AXF8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Swol_1287;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68596.1; -; Genomic_DNA.
DR   RefSeq; WP_011640698.1; NC_008346.1.
DR   AlphaFoldDB; Q0AXF8; -.
DR   SMR; Q0AXF8; -.
DR   STRING; 335541.Swol_1287; -.
DR   EnsemblBacteria; ABI68596; ABI68596; Swol_1287.
DR   KEGG; swo:Swol_1287; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_3_1_9; -.
DR   OMA; NRWYFPA; -.
DR   OrthoDB; 1575081at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001968; 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.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cell membrane; Hydrolase; Membrane; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..149
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_1000097284"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   149 AA;  16606 MW;  606DF14F648BD14A CRC64;
     MRFWGSFLLV VILDRISKAW VLASFLPRES RSLIEGGLYL TYVQNRGAAF GLMPGKSWLF
     FISALLVIMA LVIYNWRSKA SPLEALSTGL IAGGALGNLI DRYFYGFVID FIDLGWWPVF
     NLADSAIVCG GILLLILVLL DGKREERNA