ID   LSPA_NOSP7              Reviewed;         158 AA.
AC   B2IU55;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Npun_R0889;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001037; ACC79626.1; -; Genomic_DNA.
DR   RefSeq; WP_012407648.1; NC_010628.1.
DR   AlphaFoldDB; B2IU55; -.
DR   SMR; B2IU55; -.
DR   STRING; 63737.Npun_R0889; -.
DR   EnsemblBacteria; ACC79626; ACC79626; Npun_R0889.
DR   KEGG; npu:Npun_R0889; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_3_2_3; -.
DR   OMA; NRWYFPA; -.
DR   OrthoDB; 1575081at2; -.
DR   PhylomeDB; B2IU55; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001191; 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..158
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_1000097267"
FT   TRANSMEM        7..27
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        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   158 AA;  17614 MW;  40CB444AA46951A2 CRC64;
     MRLKNRLFWI AAFIAFFLDQ ITKYWVVQTF SLGQTLPLLT GIFHFTYVTN TGAAFSLLSG
     KVEWLRWLSL GVSLVLIALA LFGPTLNLWD QLGYGLILGG AMGNGIDRFV LGHVVDFLDF
     RLISFPVFNV ADSFISIGIV FLLIASFQKT PTSTGRLD