ID A0A0W0TW63_9GAMM Unreviewed; 156 AA.
AC A0A0W0TW63;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:KTC99676.1};
GN ORFNames=E4T54_10860 {ECO:0000313|EMBL:QBS13201.1}, Lgee_1168
GN {ECO:0000313|EMBL:KTC99676.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTC99676.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTC99676.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTC99676.1,
RC ECO:0000313|Proteomes:UP000054785};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBS13201.1, ECO:0000313|Proteomes:UP000294523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1308 {ECO:0000313|EMBL:QBS13201.1,
RC ECO:0000313|Proteomes:UP000294523};
RA Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA Charpentier X.;
RT "Diverse conjugative elements silence natural transformation in Legionella
RT species.";
RL Submitted (MAR-2019) 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}.
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DR EMBL; LNYC01000044; KTC99676.1; -; Genomic_DNA.
DR EMBL; CP038271; QBS13201.1; -; Genomic_DNA.
DR RefSeq; WP_028387399.1; NZ_UGNZ01000001.1.
DR AlphaFoldDB; A0A0W0TW63; -.
DR STRING; 45065.Lgee_1168; -.
DR KEGG; lgt:E4T54_10860; -.
DR PATRIC; fig|45065.4.peg.1255; -.
DR OrthoDB; 9810259at2; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
DR Proteomes; UP000294523; Chromosome.
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:KTC99676.1};
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:UP000054785};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 135
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 156 AA; 17881 MW; 80FD53588F79461A CRC64;
MKKWPWLLLS LGILVLDQLS KYWVGLHFTP WVPYPVFSGF NITLAWNNGA AFSFLSGAGE
WHRWFFVVFS LLMSVVFVIW LRRLPENAVL QPLAIALLLG GAAGNLIDRL FFGYVVDFLE
VYYQNWHWPV FNIADSAIFV GAVLLMLDLL RNKTAT
//
