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 03-SEP-2014, entry version 52. DE RecName: Full=Lipoprotein signal peptidase; DE EC=3.4.23.36; DE AltName: Full=Prolipoprotein signal peptidase; DE AltName: Full=Signal peptidase II; DE Short=SPase II; GN Name=lspA; OrderedLocusNames=MAV_3231; OS Mycobacterium avium (strain 104). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC 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 (By similarity). 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. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein CC (By similarity). CC -!- SIMILARITY: Belongs to the peptidase A8 family. 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 STRING; 243243.MAV_3231; -. DR MEROPS; A08.001; -. DR EnsemblBacteria; ABK69194; ABK69194; MAV_3231. DR GeneID; 4529480; -. DR KEGG; mav:MAV_3231; -. DR PATRIC; 17988157; VBIMycAvi38287_3163. DR eggNOG; COG0597; -. DR HOGENOM; HOG000096992; -. DR KO; K03101; -. DR OMA; FVSVGWW; -. 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; Complete proteome; Hydrolase; KW Membrane; Protease; Transmembrane; Transmembrane helix. FT CHAIN 1 182 Lipoprotein signal peptidase. FT /FTId=PRO_0000289400. FT TRANSMEM 21 41 Helical; (Potential). FT TRANSMEM 74 94 Helical; (Potential). FT TRANSMEM 98 118 Helical; (Potential). FT TRANSMEM 146 166 Helical; (Potential). FT ACT_SITE 119 119 By similarity. FT ACT_SITE 148 148 By similarity. 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 //