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LSPA_BUCAT
ID   LSPA_BUCAT              Reviewed;         160 AA.
AC   B8D753;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=BUAPTUC7_147;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001158; ACL29968.1; -; Genomic_DNA.
DR   RefSeq; WP_012619451.1; NC_011834.1.
DR   AlphaFoldDB; B8D753; -.
DR   SMR; B8D753; -.
DR   KEGG; bau:BUAPTUC7_147; -.
DR   HOGENOM; CLU_083252_4_0_6; -.
DR   OMA; IEFGMVF; -.
DR   UniPathway; UPA00665; -.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..160
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_1000123492"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   160 AA;  18693 MW;  28778C967809651D CRC64;
     MKQKYSKKSK KWIYITTIIF ILILDISSKH LIIKYIKTYD TKKIFSVLNF FHVHNHGAAF
     SFLSDQNGWQ KWFLSTVSIL TILVMTRIIT KLKKQETKKI TAYSLIIAGA TGNLIDRIFY
     GFVVDFIDIH INDWHFATFN IADCSIFIGI IILMRINYST
 
 
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