(data stored in SCRATCH zone)

HOGENOM: MESSB_1_PE100

ID   MESSB_1_PE100                        STANDARD;      PRT;   174 AA.
AC   MESSB_1_PE100; Q11N20;
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 2; EC=3.4.23 36;AltName:
DE   Full=Prolipoprotein signal peptidase 2;AltName: Full=Signal peptidase II
DE   2;Flags: Precursor; (MESSB_1.PE100).
GN   Name=lspA2; OrderedLocusNames=Meso_4211;
OS   CHELATIVORANS SP. BNC1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MESSB_1.PE100.
CC       Mesorhizobium sp. BNC1 plasmid 1, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q11N20_MESSB
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; Q11N20; -.
DR   EMBL; CP000389; ABG61188.1; -; Genomic_DNA.
DR   RefSeq; YP_665835.1; NC_008242.1.
DR   STRING; Q11N20; -.
DR   MEROPS; A08.001; -.
DR   GeneID; 4178555; -.
DR   GenomeReviews; CP000389_GR; Meso_4211.
DR   KEGG; mes:Meso_4211; -.
DR   NMPDR; fig|266779.1.peg.3634; -.
DR   eggNOG; COG0597; -.
DR   OMA; PPRTIEI; -.
DR   PhylomeDB; Q11N20; -.
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; MESSB_1.PE100; -.
KW   lipoprotein signal peptidase;
KW   Aspartyl protease; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Membrane; Plasmid; Protease; Signal;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   174 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAYPRLIRRA TLACGALAAA LAVDLVTKWL ILNVVMVPPR TIEIAPFFNL TLGFNTGVSF
     GMFREFFLDR PLMLAGIKMV IVAGLLLWAM RTPKPLETLG LGLIAGGAMG NIVDRISQGA
     VTDFLDFRIG GWHWPAFNMA DTTITIGVAL LIAGSFWPGR SVAPVLKRPS GAGH
//

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