(data stored in ACNUC7421 zone)

SWISSPROT: Q13GM9_PARXL

ID   Q13GM9_PARXL            Unreviewed;       170 AA.
AC   Q13GM9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   11-DEC-2019, entry version 111.
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   ORFNames=Bxe_A1105 {ECO:0000313|EMBL:ABE31841.1}, Bxe_A2904
GN   {ECO:0000313|EMBL:ABE30072.1}, Bxe_B1606
GN   {ECO:0000313|EMBL:ABE34358.1}, Bxe_B2910
GN   {ECO:0000313|EMBL:ABE33085.1}, Bxe_C0390
GN   {ECO:0000313|EMBL:ABE36297.1}, Bxe_C0884
GN   {ECO:0000313|EMBL:ABE36760.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36760.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36760.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36760.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
RN   [2] {ECO:0000313|EMBL:ABE30072.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE30072.1};
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., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome 1 of Burkholderia xenovorans LB400.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABE33085.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33085.1};
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., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome 2 of Burkholderia xenovorans LB400.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ABE36760.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36760.1};
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., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome 3 of Burkholderia xenovorans LB400.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC       peptides from prolipoproteins. {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS01181907}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of signal peptides from bacterial membrane
CC         prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in
CC         which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and
CC         Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00161,
CC         ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS01181912};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC       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. {ECO:0000256|HAMAP-
CC       Rule:MF_00161, ECO:0000256|RuleBase:RU004181,
CC       ECO:0000256|SAAS:SAAS01181910}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00161}.
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DR   EMBL; CP000270; ABE30072.1; -; Genomic_DNA.
DR   EMBL; CP000270; ABE31841.1; -; Genomic_DNA.
DR   EMBL; CP000271; ABE33085.1; -; Genomic_DNA.
DR   EMBL; CP000271; ABE34358.1; -; Genomic_DNA.
DR   EMBL; CP000272; ABE36297.1; -; Genomic_DNA.
DR   EMBL; CP000272; ABE36760.1; -; Genomic_DNA.
DR   RefSeq; WP_004863699.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_C0884; -.
DR   MEROPS; A08.001; -.
DR   EnsemblBacteria; ABE30072; ABE30072; Bxe_A2904.
DR   EnsemblBacteria; ABE31841; ABE31841; Bxe_A1105.
DR   EnsemblBacteria; ABE33085; ABE33085; Bxe_B2910.
DR   EnsemblBacteria; ABE34358; ABE34358; Bxe_B1606.
DR   EnsemblBacteria; ABE36297; ABE36297; Bxe_C0390.
DR   EnsemblBacteria; ABE36760; ABE36760; Bxe_C0884.
DR   GeneID; 4010397; -.
DR   KEGG; bxb:DR64_3269; -.
DR   KEGG; bxb:DR64_5241; -.
DR   KEGG; bxb:DR64_586; -.
DR   KEGG; bxb:DR64_6909; -.
DR   KEGG; bxb:DR64_7565; -.
DR   KEGG; bxb:DR64_854; -.
DR   KEGG; bxe:Bxe_A1105; -.
DR   KEGG; bxe:Bxe_A2904; -.
DR   KEGG; bxe:Bxe_B1606; -.
DR   KEGG; bxe:Bxe_B2910; -.
DR   KEGG; bxe:Bxe_C0390; -.
DR   KEGG; bxe:Bxe_C0884; -.
DR   eggNOG; ENOG4107TEJ; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096993; -.
DR   KO; K03101; -.
DR   OMA; IEFGMVF; -.
DR   OrthoDB; 1575081at2; -.
DR   BioCyc; BXEN266265:BXE_RS07605-MONOMER; -.
DR   BioCyc; BXEN266265:BXE_RS16425-MONOMER; -.
DR   BioCyc; BXEN266265:BXE_RS22650-MONOMER; -.
DR   BioCyc; BXEN266265:BXE_RS29075-MONOMER; -.
DR   BioCyc; BXEN266265:BXE_RS38530-MONOMER; -.
DR   BioCyc; BXEN266265:BXE_RS40860-MONOMER; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001817; Chromosome 3.
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; Q13GM9.
DR   SWISS-2DPAGE; Q13GM9.
KW   Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, 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   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU000594,
KW   ECO:0000256|SAAS:SAAS01181933, ECO:0000313|EMBL:ABE36760.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|SAAS:SAAS01181906};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU000594,
KW   ECO:0000256|SAAS:SAAS01181905};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..170
FT                   /note="Lipoprotein signal peptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015097025"
FT   TRANSMEM        68..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   170 AA;  18815 MW;  ECE1C7415B3C10FB CRC64;
     MLIIGKKLSP YALLSISGLL AASDQAVKWL VQQSMAYGEY VSVTPFFNWV HLWNTGAAFS
     LFANGGGWQR YFFIGIAVVV SIFLIKLILE NRHKGEAIAY SLILGGAMGN LIDRVFRGYV
     VDSFDFYWRD WHWPAFNLAD IAIVLGALLF VSSSLLGKKA NTNAEPDGSD
//

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