(data stored in ACNUC7421 zone)

HOGENOM: ACCPU_3_PE139

ID   ACCPU_3_PE139                        STANDARD;      PRT;   359 AA.
AC   ACCPU_3_PE139; C7RW30;
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   SubName: Full=Lipoprotein signal peptidase; (ACCPU_3.PE139).
GN   OrderedLocusNames=CAP2UW1_4506, CAP2UW1_4567, CAP2UW1_4717;
OS   CANDIDATUS ACCUMULIBACTER PHOSPHATIS CLADE IIA STR. UW-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=522306;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACCPU_3.PE139.
CC       Candidatus Accumulibacter phosphatis clade IIA str. UW-1 plasmid pAph01
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7RW30_ACCPU
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   -!- GENE_FAMILY: HOG000002872 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C7RW30; -.
DR   EMBL; CP001716; ACV37840.1; -; Genomic_DNA.
DR   EMBL; CP001717; ACV37897.1; -; Genomic_DNA.
DR   EMBL; CP001718; ACV37922.1; -; Genomic_DNA.
DR   RefSeq; YP_003162888.1; NC_013190.1.
DR   RefSeq; YP_003162913.1; NC_013191.1.
DR   RefSeq; YP_003165287.1; NC_013193.1.
DR   STRING; C7RW30; -.
DR   MEROPS; A08.001; -.
DR   GeneID; 8401824; -.
DR   GeneID; 8401850; -.
DR   GeneID; 8402079; -.
DR   GenomeReviews; CP001716_GR; CAP2UW1_4506.
DR   GenomeReviews; CP001717_GR; CAP2UW1_4567.
DR   GenomeReviews; CP001718_GR; CAP2UW1_4717.
DR   KEGG; app:CAP2UW1_4506; -.
DR   KEGG; app:CAP2UW1_4567; -.
DR   KEGG; app:CAP2UW1_4717; -.
DR   ProtClustDB; CLSK923962; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
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; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR001872; Peptidase_A8.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
DR   TIGRFAMs; TIGR00077; LspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
DR   HOGENOMDNA; ACCPU_3.PE139; -.
KW   hypothetical protein;
KW   Aspartyl protease; Cell membrane; Complete proteome; Hydrolase;
KW   Lipoprotein; Membrane; Plasmid; Protease; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   359 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSWKFFLYDW GGLNIALFQA INMSTPAALE PPVSFFNLVI GNYWTAPLML LAMWGWSKSA
     PDPTRADAIR YRLRVFSVAF ALAFLVATIL KLWIDFPRPP AVFGDMVRVI GGIERHYSLP
     SGHATYAALV VGALWPLIGR RGRIGLVLYA ALVGWSRIAA GMHFPADVLA GWVLGLSCTA
     LAGWLMPLAA PVWQSARRTS TWVWFAVAAS SVMTDQLAKF AITRTFAYGE QVEVSTFFNI
     VHVLNPGAAF SFLANAGGWQ RYFLMALGLV VSAWLGRMLC QQRPRLEAVG YSLILGGALG
     NVVDRVLRGS VVDFLDFHWQ LVHWPAFNLA DVAITIGALC LFLTVVPKSS RGTEADVSG
//

If you have problems or comments...

PBIL Back to PBIL home page