(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE3553

ID   ACAM1_1_PE3553                       STANDARD;      PRT;   165 AA.
AC   ACAM1_1_PE3553; B0C3E3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Lipoprotein signal peptidase; EC=3.4.23 36;AltName:
DE   Full=Prolipoprotein signal peptidase;AltName: Full=Signal peptidase II;
DE   Short=SPase II; (ACAM1_1.PE3553).
GN   Name=lspA; OrderedLocusNames=AM1_3652;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE3553.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:LSPA_ACAM1
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins (By similarity).
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: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC   -!- GENE_FAMILY: HOG000096992 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0C3E3; -.
DR   EMBL; CP000828; ABW28642.1; -; Genomic_DNA.
DR   RefSeq; YP_001517958.1; NC_009925.1.
DR   STRING; B0C3E3; -.
DR   MEROPS; A08.001; -.
DR   GeneID; 5682458; -.
DR   GenomeReviews; CP000828_GR; AM1_3652.
DR   KEGG; amr:AM1_3652; -.
DR   OMA; IASEIHG; -.
DR   ProtClustDB; PRK00376; -.
DR   BioCyc; AMAR329726:AM1_3652-MON; -.
DR   GO; GO:0016021; C:integral to 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-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_00161; LspA; 1; -.
DR   InterPro; IPR001872; Peptidase_A8.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   TIGRFAMs; TIGR00077; LspA; 1.
DR   PROSITE; PS00855; SPASE_II; FALSE_NEG.
DR   HOGENOMDNA; ACAM1_1.PE3553; -.
KW   lipoprotein signal peptidase;
KW   Aspartyl protease; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Membrane; Protease; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   165 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRWKKLLFWG SALLSVGADQ LTKFWVTQNF ELRRPPAQPD TWPLIQNVFH FTYVTNDGAA
     FSLFKDSPLL PWLSFLVCLG LIGLGLFGPR FPQWEQAGYG FLLGGAAGNG IDRIFLGEVI
     DFLDFRLIQF PVFNIADISI NVGLACLIFA TWQSSRKGSR KTPTP
//

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