LSPA_VIBCM
ID LSPA_VIBCM Reviewed; 171 AA.
AC C3LST8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161};
DE AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161};
DE Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161};
GN Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161}; OrderedLocusNames=VCM66_0641;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC peptides from prolipoproteins. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00161};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00161}.
CC -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP-
CC Rule:MF_00161}.
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DR EMBL; CP001233; ACP04964.1; -; Genomic_DNA.
DR RefSeq; WP_000071968.1; NC_012578.1.
DR AlphaFoldDB; C3LST8; -.
DR SMR; C3LST8; -.
DR MEROPS; A08.001; -.
DR EnsemblBacteria; ACP04964; ACP04964; VCM66_0641.
DR GeneID; 57739398; -.
DR KEGG; vcm:VCM66_0641; -.
DR HOGENOM; CLU_083252_4_0_6; -.
DR OMA; NRWYFPA; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000001217; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR33695; 1.
DR Pfam; PF01252; Peptidase_A8; 1.
DR PRINTS; PR00781; LIPOSIGPTASE.
DR TIGRFAMs; TIGR00077; lspA; 1.
DR PROSITE; PS00855; SPASE_II; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..171
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_1000123506"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 128
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 171 AA; 19390 MW; 4100310F3E1CD460 CRC64;
MSNSSLALKQ SGLRWLWLAL LVFIADITIK LIVMDNMGYG WANRIEVLPF FNLLYVHNYG
AAFSFLSDQE GWQRWLFTGI AFVVTGMLAY WMRRLPASDK WNNIAYALII GGAVGNVFDR
IVHGFVVDYL DFYWGTYHWP AFNLADSTIC IGAAMIILDG FRAKKSAPSQ S