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Database: UniProt
Entry: A0A374VBA8_9BACE
LinkDB: A0A374VBA8_9BACE
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ID   A0A374VBA8_9BACE        Unreviewed;       224 AA.
AC   A0A374VBA8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=DXC10_10720 {ECO:0000313|EMBL:RGM46846.1};
OS   Bacteroides sp. OM08-11.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=2292284 {ECO:0000313|EMBL:RGM46846.1, ECO:0000313|Proteomes:UP000262405};
RN   [1] {ECO:0000313|EMBL:RGM46846.1, ECO:0000313|Proteomes:UP000262405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM08-11 {ECO:0000313|EMBL:RGM46846.1,
RC   ECO:0000313|Proteomes:UP000262405};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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   -!- 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   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC       cleavage). {ECO:0000256|HAMAP-Rule:MF_00161}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|RuleBase:RU004181}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00161}.
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:RGM46846.1}.
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DR   EMBL; QSTJ01000005; RGM46846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A374VBA8; -.
DR   OrthoDB; 9810259at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000262405; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00161; LspA; 1.
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.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750, ECO:0000256|HAMAP-
KW   Rule:MF_00161};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00161};
KW   Lipoprotein {ECO:0000313|EMBL:RGM46846.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262405};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        109..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        185..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   224 AA;  25678 MW;  F113AC097E64C1EA CRC64;
     MKKFFTKGRI ALLVIFSVLI VDQVIKVVVK TQMYWHQSEN VIKWIYEKFG IVDAEPPTWF
     YIYFTENNGM AFGMEIFGKL FLTLFRIVAV AIIGWFLYKF IKKGLKTGFI VCISLVLTGA
     LGNIIDSIFY GVLFNESTYS QLATFMPEGG GYAPLFYGKV VDMFYFPIID TTWPQWMPFV
     GGNHFIFFSP IFNFADAAIS CGIIALLLFY SKYLNEAYHV VSKS
//
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