ID A0A174EJZ4_9FIRM Unreviewed; 168 AA.
AC A0A174EJZ4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ECO:0000313|EMBL:CUO36719.1};
GN ORFNames=DW021_04710 {ECO:0000313|EMBL:RHL49648.1}, DW272_03500
GN {ECO:0000313|EMBL:RHG20284.1}, DWW07_04710
GN {ECO:0000313|EMBL:RGV65855.1}, DWX77_03685
GN {ECO:0000313|EMBL:RGS75466.1}, DWZ12_06820
GN {ECO:0000313|EMBL:RGQ05598.1}, ERS852394_02039
GN {ECO:0000313|EMBL:CUO36719.1};
OS Blautia obeum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=40520 {ECO:0000313|EMBL:CUO36719.1, ECO:0000313|Proteomes:UP000095409};
RN [1] {ECO:0000313|EMBL:CUO36719.1, ECO:0000313|Proteomes:UP000095409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUO36719.1,
RC ECO:0000313|Proteomes:UP000095409};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000265828, ECO:0000313|Proteomes:UP000283585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF14-23 {ECO:0000313|EMBL:RGV65855.1,
RC ECO:0000313|Proteomes:UP000265828}, AF21-24
RC {ECO:0000313|EMBL:RGS75466.1, ECO:0000313|Proteomes:UP000284242},
RC AF29-2BH {ECO:0000313|EMBL:RGQ05598.1,
RC ECO:0000313|Proteomes:UP000283585}, AF37-6AC
RC {ECO:0000313|EMBL:RHL49648.1, ECO:0000313|Proteomes:UP000285897}, and
RC AM22-9LB {ECO:0000313|EMBL:RHG20284.1,
RC ECO:0000313|Proteomes:UP000284220};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYZD01000009; CUO36719.1; -; Genomic_DNA.
DR EMBL; QRSS01000006; RGQ05598.1; -; Genomic_DNA.
DR EMBL; QRVV01000006; RGS75466.1; -; Genomic_DNA.
DR EMBL; QRZI01000002; RGV65855.1; -; Genomic_DNA.
DR EMBL; QRHZ01000001; RHG20284.1; -; Genomic_DNA.
DR EMBL; QROS01000002; RHL49648.1; -; Genomic_DNA.
DR RefSeq; WP_022389334.1; NZ_SPFW01000010.1.
DR AlphaFoldDB; A0A174EJZ4; -.
DR GeneID; 79804152; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000095409; Unassembled WGS sequence.
DR Proteomes; UP000265828; Unassembled WGS sequence.
DR Proteomes; UP000283585; Unassembled WGS sequence.
DR Proteomes; UP000284220; Unassembled WGS sequence.
DR Proteomes; UP000284242; Unassembled WGS sequence.
DR Proteomes; UP000285897; 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 NCBIfam; TIGR00077; lspA; 1.
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:CUO36719.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00161};
KW Reference proteome {ECO:0000313|Proteomes:UP000095409};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 134..158
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 168 AA; 18911 MW; 19096247D38C76F7 CRC64;
MNKKKASFIC FLVWFTGIIL LIVADQAAKY WAVSKLKGTS GMTLITGVLE LQYLENRGMA
FGMLQGRQML FLVLCIAFCA VMLWLFFRIP KTGYYIPLIL AGGILTGGAA GNFIDRAFRG
YVVDFIYVSL IDFPIFNLAD IYVVCGGIAL VILVLFHYRD EDFDFIKK
//
