(data stored in ACNUC7421 zone)

SWISSPROT: LSPA_ECODH

ID   LSPA_ECODH              Reviewed;         164 AA.
AC   B1XBF2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 58.
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=ECDH10B_0028;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01232.1; -; Genomic_DNA.
DR   RefSeq; WP_000083372.1; NC_010473.1.
DR   ProteinModelPortal; B1XBF2; -.
DR   SMR; B1XBF2; -.
DR   EnsemblBacteria; ACB01232; ACB01232; ECDH10B_0028.
DR   KEGG; ecd:ECDH10B_0028; -.
DR   eggNOG; ENOG4105M02; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096993; -.
DR   KO; K03101; -.
DR   OMA; NRWYFPA; -.
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-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; B1XBF2.
DR   SWISS-2DPAGE; B1XBF2.
KW   Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase;
KW   Membrane; Protease; Transmembrane; Transmembrane helix.
FT   CHAIN         1    164       Lipoprotein signal peptidase.
FT                                /FTId=PRO_1000097253.
FT   TRANSMEM     12     32       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM     70     90       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM    102    122       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM    137    157       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
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;  18156 MW;  65773737DDAA3EB1 CRC64;
     MSQSICSTGL RWLWLVVVVL IIDLGSKYLI LQNFALGDTV PLFPSLNLHY ARNYGAAFSF
     LADSGGWQRW FFAGIAIGIS VILAVMMYRS KATQKLNNIA YALIIGGALG NLFDRLWHGF
     VVDMIDFYVG DWHFATFNLA DTAICVGAAL IVLEGFLPSR AKKQ
//

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