LSPA_STAES
ID LSPA_STAES Reviewed; 161 AA.
AC Q8CPK0;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=SE_0871;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO04468.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015929; AAO04468.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_764426.1; NC_004461.1.
DR RefSeq; WP_002494957.1; NC_004461.1.
DR AlphaFoldDB; Q8CPK0; -.
DR SMR; Q8CPK0; -.
DR STRING; 176280.SE_0871; -.
DR EnsemblBacteria; AAO04468; AAO04468; SE_0871.
DR GeneID; 50018990; -.
DR KEGG; sep:SE_0871; -.
DR PATRIC; fig|176280.10.peg.844; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_3_0_9; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000001411; 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..161
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_0000178820"
FT TRANSMEM 9..29
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 161 AA; 18235 MW; 997929A6BCA7BA53 CRC64;
MKKKYYISIS LLMTIIVLVF DQVSKWLITI SMKVGDSYEI IPNFLNITSH RNNGAAWGIL
SGKMLFFYII TIIILIVLVI FYIKEAQFNL FMQVAISLLF AGALGNFIDR VLHGEVVDFI
DTNIFGYDFP IFNIADSSLT IGVIFVIIAL IKDAIINKKE V