ID A0A1U7M312_TISCR Unreviewed; 151 AA.
AC A0A1U7M312;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_2 {ECO:0000313|EMBL:OLS01697.1};
GN Synonyms=lspA {ECO:0000256|HAMAP-Rule:MF_00161};
GN ORFNames=TICRE_22970 {ECO:0000313|EMBL:OLS01697.1};
OS Tissierella creatinophila DSM 6911.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1123403 {ECO:0000313|EMBL:OLS01697.1, ECO:0000313|Proteomes:UP000186112};
RN [1] {ECO:0000313|EMBL:OLS01697.1, ECO:0000313|Proteomes:UP000186112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6911 {ECO:0000313|EMBL:OLS01697.1,
RC ECO:0000313|Proteomes:UP000186112};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Tissierella creatinophila DSM 6911.";
RL Submitted (FEB-2016) 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:OLS01697.1}.
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DR EMBL; LTDM01000064; OLS01697.1; -; Genomic_DNA.
DR RefSeq; WP_075728175.1; NZ_LTDM01000064.1.
DR AlphaFoldDB; A0A1U7M312; -.
DR OrthoDB; 9810259at2; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000186112; 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:OLS01697.1};
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:UP000186112};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 121..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 111
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 151 AA; 17575 MW; D43574ED75E9E8D6 CRC64;
MEFFLIAFIV FADQISKYGA IRYLKNRRPY VVLENFLQLN YVENRGAAFG ILEHKRLFFI
IITLAIIIFL SFYMIKNYNN LSIFTRISFS ILIAGAAGNL IDRIRLGYVV DFISFRLKGY
YNFPVFNIAD TFIVISTILV VIIILFDKIE A
//
