ID   LSPA_ENTAE     STANDARD;      PRT;   165 AA.
AC   P13514;
DT   01-JAN-1990 (Rel. 13, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Lipoprotein signal peptidase (EC 3.4.23.36) (Prolipoprotein signal
DE   peptidase) (Signal peptidase II) (SPase II).
GN   Name=lspA; Synonyms=lsp;
OS   Enterobacter aerogenes (Aerobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 13048;
RX   MEDLINE=90094256; PubMed=2403548;
RA   Isaki L., Kawakami M., Beers R., Hom R., Wu H.C.;
RT   "Cloning and nucleotide sequence of the Enterobacter aerogenes signal
RT   peptidase II (lsp) gene.";
RL   J. Bacteriol. 172:469-472(1990).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins.
CC   -!- CATALYTIC ACTIVITY: Release of signal peptides from bacterial
CC       membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-
CC       (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably
CC       Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small,
CC       neutral side chains.
CC   -!- PATHWAY: Lipoprotein biosynthesis; second step.
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein. Inner membrane
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M26713; AAA24804.1; -.
DR   MEROPS; A08.001; -.
DR   HAMAP; MF_00161; -; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   ProDom; PD004304; Peptidase_A8; 1.
DR   TIGRFAMs; TIGR00077; lspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
KW   Aspartyl protease; Hydrolase; Inner membrane; Transmembrane.
FT   DOMAIN        1     11       Cytoplasmic (Potential).
FT   TRANSMEM     12     22       Potential.
FT   DOMAIN       23     69       Periplasmic (Potential).
FT   TRANSMEM     70     88       Potential.
FT   DOMAIN       89     95       Cytoplasmic (Potential).
FT   TRANSMEM     96    113       Potential.
FT   DOMAIN      114    138       Periplasmic (Potential).
FT   TRANSMEM    139    153       Potential.
FT   DOMAIN      154    165       Cytoplasmic (Potential).
FT   ACT_SITE    114    114       By similarity.
FT   ACT_SITE    141    141       By similarity.
SQ   SEQUENCE   165 AA;  18107 MW;  A47A352CB1616724 CRC64;
     MSKSICSTGL RWLWVVVAVL IIDLGSKFLI LQNFALGETV SLFPSLNLHY ARNYGAAFSF
     LADSGGWQRW FFAGIAVGIC VVLAVLMYRS KATQKLNNIA YALIIGGALG NLFDRLWHGF
     VVDMIDFYVG DWHFATFNLA DSAICIGAAL IVLEGFLPSS DKKTS
//