(data stored in ACNUC7421 zone)

SWISSPROT: LSPA_ECO57

ID   LSPA_ECO57              Reviewed;         164 AA.
AC   Q8XA48;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 93.
DE   RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE            EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161};
DE            Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161};
GN   Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161};
GN   OrderedLocusNames=Z0031, ECs0030;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins. {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
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. {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00161}.
DR   EMBL; AE005174; AAG54329.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33453.1; -; Genomic_DNA.
DR   PIR; E85483; E85483.
DR   PIR; F90632; F90632.
DR   RefSeq; NP_308057.1; NC_002695.1.
DR   RefSeq; WP_000083385.1; NZ_MWVM01000003.1.
DR   SMR; Q8XA48; -.
DR   STRING; 155864.Z0031; -.
DR   EnsemblBacteria; AAG54329; AAG54329; Z0031.
DR   EnsemblBacteria; BAB33453; BAB33453; BAB33453.
DR   GeneID; 913426; -.
DR   KEGG; ece:Z0031; -.
DR   KEGG; ecs:ECs0030; -.
DR   PATRIC; fig|386585.9.peg.125; -.
DR   eggNOG; ENOG4105M02; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096993; -.
DR   KO; K03101; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of 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   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695:SF2; PTHR33695:SF2; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   TIGRFAMs; TIGR00077; lspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XA48.
DR   SWISS-2DPAGE; Q8XA48.
KW   Aspartyl protease; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Membrane; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    164       Lipoprotein signal peptidase.
FT                                /FTId=PRO_0000178780.
FT   TOPO_DOM      1     11       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     12     26       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TOPO_DOM     27     69       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     70     88       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TOPO_DOM     89     95       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     96    113       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TOPO_DOM    114    141       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    142    159       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TOPO_DOM    160    164       Cytoplasmic. {ECO:0000255}.
FT   ACT_SITE    114    114       {ECO:0000255|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    141    141       {ECO:0000255|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   164 AA;  18144 MW;  50D8C5B08F58A15B CRC64;
     MSQSICSTGL RWLWLVVVVL IIDLGSKYLI LQNFALGDTV PLFPSLNLHY ARNYGAAFSF
     LADSGGWQRW FFAGIAIGIS VTLVVMMYRS KATQKLNNIA YALIIGGALG NLFDRLWHGF
     VVDMIDFYVG DWHFATFNLA DTAICVGAAL IVLEGFLPSK AKKQ
//

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