ID A0A0K8NVE5_IDESA Unreviewed; 76 AA.
AC A0A0K8NVE5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Lipoprotein signal peptidase {ECO:0000313|EMBL:GAP34239.1};
DE EC=3.4.23.36 {ECO:0000313|EMBL:GAP34239.1};
GN ORFNames=ISF6_4018 {ECO:0000313|EMBL:GAP34239.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP34239.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP34239.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
CC -!- SIMILARITY: Belongs to the peptidase A8 family.
CC {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|RuleBase:RU004181}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAP34239.1}.
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DR EMBL; BBYR01000006; GAP34239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8NVE5; -.
DR STRING; 1547922.ISF6_4018; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR001872; Peptidase_A8.
DR PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR Pfam; PF01252; Peptidase_A8; 1.
DR PRINTS; PR00781; LIPOSIGPTASE.
DR PROSITE; PS00855; SPASE_II; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAP34239.1};
KW Lipoprotein {ECO:0000313|EMBL:GAP34239.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037660}.
SQ SEQUENCE 76 AA; 7938 MW; 762CC2988AFF84C4 CRC64;
MRHLEALAYS LILGGALGNA FDRVARGQVI DYLDFHLRGV HWPAFNIADM AITGGAVVLA
SLLGYGDAKP ASPAGS
//
