ID   LSPA_ACIAD              Reviewed;         179 AA.
AC   Q6FG03;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 123.
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=ACIAD0021;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67004.1; -; Genomic_DNA.
DR   RefSeq; WP_004930972.1; NC_005966.1.
DR   AlphaFoldDB; Q6FG03; -.
DR   SMR; Q6FG03; -.
DR   STRING; 202950.GCA_001485005_01769; -.
DR   GeneID; 45232555; -.
DR   KEGG; aci:ACIAD0021; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_4_0_6; -.
DR   OrthoDB; 9810259at2; -.
DR   BioCyc; ASP62977:ACIAD_RS00115-MONOMER; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000000430; Chromosome.
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:InterPro.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   NCBIfam; TIGR00077; lspA; 1.
DR   PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
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..179
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_0000289348"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   179 AA;  20370 MW;  486C730BBC6042E0 CRC64;
     MPKLEAKKGL FQFYPHNLIW LGLSILAIII DQWTKWIAST HLNYADPVPV LPFLNWTLLH
     NYGAAFSFLS DAGGWQHYLF TGLAGIVSII FIFWLMRMPK NAMILPAAIA LILGGALGNL
     IDRMTLGYVV DFIHIYYQNH HFPAFNIADS AITIGTILLL IDTFFLEKQR IQRAEVKHD
//