(data stored in ACNUC7421 zone)

SWISSPROT: A0LEH4_SYNFM

ID   A0LEH4_SYNFM            Unreviewed;       153 AA.
AC   A0LEH4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Lipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161};
DE            EC=3.4.23.36 {ECO:0000256|HAMAP-Rule:MF_00161};
DE   AltName: Full=Prolipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161};
DE   AltName: Full=Signal peptidase II {ECO:0000256|HAMAP-Rule:MF_00161};
DE            Short=SPase II {ECO:0000256|HAMAP-Rule:MF_00161};
GN   Name=lspA {ECO:0000256|HAMAP-Rule:MF_00161};
GN   OrderedLocusNames=Sfum_0123 {ECO:0000313|EMBL:ABK15826.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15826.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15826.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins. {ECO:0000256|HAMAP-
CC       Rule:MF_00161, ECO:0000256|SAAS:SAAS01181907}.
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:0000256|HAMAP-
CC         Rule:MF_00161, ECO:0000256|SAAS:SAAS01181912};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage). {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|SAAS:SAAS01181909}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU004181,
CC       ECO:0000256|SAAS:SAAS01181910}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00161}.
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DR   EMBL; CP000478; ABK15826.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0123; -.
DR   MEROPS; A08.001; -.
DR   EnsemblBacteria; ABK15826; ABK15826; Sfum_0123.
DR   KEGG; sfu:Sfum_0123; -.
DR   eggNOG; ENOG4107TEJ; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096992; -.
DR   KO; K03101; -.
DR   OMA; RADNAVE; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001784; 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-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.
PE   3: Inferred from homology;
DR   PRODOM; A0LEH4.
DR   SWISS-2DPAGE; A0LEH4.
KW   Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181908};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181901};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181933, ECO:0000313|EMBL:ABK15826.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181906};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181905};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181903};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181900}.
FT   TRANSMEM     63     82       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     89    106       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    126    150       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   ACT_SITE    108    108       {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    135    135       {ECO:0000256|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   153 AA;  16817 MW;  D95D280CC6679497 CRC64;
     MVFLVAVAGT IILLDQLTKL LILYYVPVNT GHVVIPGFFN LIHVRNTGGA FSMLAGADAT
     WRLPFFVAMT LIVVGIIVWA YRKIDRRELW TRTAYALICG GALGNLSDRL RFGEVVDFLE
     FHIGTYSWPA FNVGDSAISA GAVMLIIALL RGK
//

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