(data stored in ACNUC7421 zone)

HOGENOM: SHEVD_1_PE1003

ID   SHEVD_1_PE1003                       STANDARD;      PRT;   167 AA.
AC   SHEVD_1_PE1003; D4ZH25;
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   (SHEVD_1.PE1003).
GN   Name=lspA; OrderedLocusNames=SVI_1003;
OS   SHEWANELLA VIOLACEA DSS12.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEVD_1.PE1003.
CC       Shewanella violacea DSS12 chromosome, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:D4ZH25_SHEVD
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: HOG000096993 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D4ZH25; -.
DR   EMBL; AP011177; BAJ00974.1; -; Genomic_DNA.
DR   RefSeq; YP_003555752.1; NC_014012.1.
DR   MEROPS; A08.001; -.
DR   GeneID; 8968622; -.
DR   GenomeReviews; AP011177_GR; SVI_1003.
DR   KEGG; svo:SVI_1003; -.
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:HAMAP.
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; 1.
DR   HOGENOMDNA; SHEVD_1.PE1003; -.
KW   lipoprotein signal peptidase;
KW   Aspartyl protease; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Lipoprotein; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   167 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRLYWVVVLV FIADQVSKQW VLANFDLYES VKLLPIFSFT YVRNYGAAFS FLSDAGGWQK
     WLFTFIAVGF SALLTFWLRK QPRQMWRLNL AYTLVIGGAL GNLIDRLQHG YVVDFLDFYW
     DKSHFPAFNI ADSAICVGAV LIILDSFISD RLEKQKKAQD EKSAAKE
//

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