ID LSPA_MYCA1 Reviewed; 182 AA. AC A0QHM5; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 24-JUN-2015, entry version 58. 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}; GN OrderedLocusNames=MAV_3231; OS Mycobacterium avium (strain 104). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=243243; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=104; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This protein specifically catalyzes the removal of CC signal peptides from prolipoproteins. {ECO:0000255|HAMAP- CC Rule:MF_00161}. CC -!- CATALYTIC ACTIVITY: Release of signal peptides from bacterial CC membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|- CC (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably CC Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, CC neutral side chains. {ECO:0000255|HAMAP-Rule:MF_00161}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}. CC -!- SUBCELLULAR LOCATION: Cell 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. CC {ECO:0000255|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; CP000479; ABK69194.1; -; Genomic_DNA. DR RefSeq; WP_011725343.1; NC_008595.1. DR RefSeq; YP_882413.1; NC_008595.1. DR EnsemblBacteria; ABK69194; ABK69194; MAV_3231. DR KEGG; mav:MAV_3231; -. DR PATRIC; 17988157; VBIMycAvi38287_3163. DR eggNOG; COG0597; -. DR HOGENOM; HOG000096992; -. DR KO; K03101; -. DR OMA; SIFGYDF; -. DR OrthoDB; EOG63NMQC; -. DR BioCyc; MAVI243243:GH3Y-3231-MONOMER; -. DR UniPathway; UPA00665; -. 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-HAMAP. DR HAMAP; MF_00161; LspA; 1. DR InterPro; IPR001872; Peptidase_A8. 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 membrane; Hydrolase; Membrane; Protease; KW Transmembrane; Transmembrane helix. FT CHAIN 1 182 Lipoprotein signal peptidase. FT /FTId=PRO_0000289400. FT TRANSMEM 21 41 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 74 94 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 98 118 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 146 166 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT ACT_SITE 119 119 {ECO:0000255|HAMAP-Rule:MF_00161}. FT ACT_SITE 148 148 {ECO:0000255|HAMAP-Rule:MF_00161}. SQ SEQUENCE 182 AA; 19621 MW; B8DDA3316CCDC18D CRC64; MPEEPTGSTA PQDRPPRRLR LLLSVAATVL ALDIVTKVLA VKLLPPGQPV PIIGDTVTWT LVRNSGAAFS MATGYTWVLT LIATGVVVGI FWMGRRLVSP WWAVGLGMIL GGAMGNLVDR FFRAPGPLRG HVVDFLSVGW WPVFNVADPS VVGGAILLVV LSIFGYDFDT VGRRKKADQS RD //