ID   LSPA_HELPH              Reviewed;         157 AA.
AC   Q1CV80;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=HPAG1_0075;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(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 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; CP000241; ABF84142.1; -; Genomic_DNA.
DR   RefSeq; WP_000921377.1; NC_008086.1.
DR   AlphaFoldDB; Q1CV80; -.
DR   SMR; Q1CV80; -.
DR   KEGG; hpa:HPAG1_0075; -.
DR   HOGENOM; CLU_083252_4_3_7; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000008835; 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:UniProtKB-KW.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..157
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_0000289391"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   157 AA;  17895 MW;  102B1B0793D92F80 CRC64;
     MLKTTKKSLL VFMGGFFLIF GVDQAIKYAI LEGFRYESLM VDIVLVFNKG VAFSLLSFLE
     GGLKYLQILL ILGLFIFLIR QIELFKTHAI EFGMVFGAGV SNVLDRFVHG GVVDYVYYHY
     GFDFAIFNFA DVMIDVGVGV LLLRQFFFKQ KQNKIKA
//