(data stored in ACNUC29543 zone)

SWISSPROT: LSPA_ACIBT

ID   LSPA_ACIBT              Reviewed;         176 AA.
AC   A3M0S2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   16-JAN-2019, entry version 71.
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=A1S_0019;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins. {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of signal peptides from bacterial membrane
CC         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.; EC=3.4.23.36; Evidence={ECO:0000255|HAMAP-
CC         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; CP000521; ABO10516.2; -; Genomic_DNA.
DR   SMR; A3M0S2; -.
DR   EnsemblBacteria; ABO10516; ABO10516; A1S_0019.
DR   KEGG; acb:A1S_0019; -.
DR   HOGENOM; HOG000096993; -.
DR   KO; K03101; -.
DR   UniPathway; UPA00665; -.
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-UniRule.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695; PTHR33695; 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; A3M0S2.
DR   SWISS-2DPAGE; A3M0S2.
KW   Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase;
KW   Membrane; Protease; Transmembrane; Transmembrane helix.
FT   CHAIN         1    176       Lipoprotein signal peptidase.
FT                                /FTId=PRO_1000097226.
FT   TRANSMEM     10     30       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM     48     68       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM     78     98       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM    102    122       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM    141    161       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   ACT_SITE    122    122       {ECO:0000255|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    149    149       {ECO:0000255|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   176 AA;  19911 MW;  CE10C08C4733E40A CRC64;
     MPNSQAKKGL FQFYPHNLIW LGLSVLAIVL DQWTKWIAST HLNYADPVPV LPFLNWTLLH
     NYGAAFSFLS DAGGWQRYFF TSLAGLVSIL FVFWLLRMPK KMVVLPVAIA LILGGALGNL
     IDRITLGYVV DFIHVYYQNH HFPAFNIADS AITLGTILLL IDTFFLEKQR PKNSDA
//

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