ID   LSPA_STAA8              Reviewed;         163 AA.
AC   Q2FZ79;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
GN   OrderedLocusNames=SAOUHSC_01162;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; CP000253; ABD30270.1; -; Genomic_DNA.
DR   RefSeq; WP_000549207.1; NZ_LS483365.1.
DR   RefSeq; YP_499702.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZ79; -.
DR   SMR; Q2FZ79; -.
DR   STRING; 1280.SAXN108_1194; -.
DR   EnsemblBacteria; ABD30270; ABD30270; SAOUHSC_01162.
DR   GeneID; 3920914; -.
DR   KEGG; sao:SAOUHSC_01162; -.
DR   PATRIC; fig|93061.5.peg.1065; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_3_0_9; -.
DR   OMA; NRWYFPA; -.
DR   UniPathway; UPA00665; -.
DR   PRO; PR:Q2FZ79; -.
DR   Proteomes; UP000008816; 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..163
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_0000289432"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   163 AA;  18342 MW;  B9D42A904F0BF33F CRC64;
     MHKKYFIGTS ILIAVFVVIF DQVTKYIIAT TMKIGDSFEV IPHFLNITSH RNNGAAWGIL
     SGKMTFFFII TIIILIALVY FFIKDAQYNL FMQVAISLLF AGALGNFIDR ILTGEVVDFI
     DTNIFGYDFP IFNIADSSLT IGVILIIIAL LKDTSNKKEK EVK