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 11-DEC-2019, entry version 76. 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=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 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 membrane {ECO:0000255|HAMAP-Rule:MF_00161}; CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161}. CC -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP- CC 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 SMR; A0QHM5; -. DR MEROPS; A08.001; -. DR EnsemblBacteria; ABK69194; ABK69194; MAV_3231. DR KEGG; mav:MAV_3231; -. DR HOGENOM; HOG000096992; -. DR KO; K03101; -. DR OMA; NRWYFPA; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000001574; Chromosome. 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 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 membrane; Hydrolase; Membrane; Protease; KW Transmembrane; Transmembrane helix. FT CHAIN 1..182 FT /note="Lipoprotein signal peptidase" FT /id="PRO_0000289400" FT TRANSMEM 21..41 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161" FT TRANSMEM 146..166 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161" FT ACT_SITE 119 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161" FT ACT_SITE 148 FT /evidence="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 //