ID   LSPA_DICNV              Reviewed;         154 AA.
AC   A5EWT1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=DNO_0084;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ13650.1; -; Genomic_DNA.
DR   RefSeq; WP_011927836.1; NC_009446.1.
DR   AlphaFoldDB; A5EWT1; -.
DR   SMR; A5EWT1; -.
DR   STRING; 246195.DNO_0084; -.
DR   EnsemblBacteria; ABQ13650; ABQ13650; DNO_0084.
DR   KEGG; dno:DNO_0084; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_3_1_6; -.
DR   OMA; NRWYFPA; -.
DR   OrthoDB; 1575081at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000000248; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..154
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_1000071545"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        66..86
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        129..149
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   154 AA;  17751 MW;  CB486E76D2D89225 CRC64;
     MNWAKRSAFF LISVACFLAD YYSKYWALTE LGARKIVVNT YMNFILAFNH GAAFSFLARA
     GGWQRWLFAG FAGIVALWLI MTLLTKSHHW LMSVSYACIL GGAVGNLYDR VVYGYVIDFI
     QWHYRTFYWP VFNLADVAIT LGVILMLIAE LHRR