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 29-APR-2008, entry version 11. DE Lipoprotein signal peptidase (EC 3.4.23.36) (Prolipoprotein signal DE peptidase) (Signal peptidase II) (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]. 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; YP_882413.1; -. DR MEROPS; A08.001; -. DR GeneID; 4529480; -. DR GenomeReviews; CP000479_GR; MAV_3231. DR KEGG; mav:MAV_3231; -. DR TIGR; MAV_3231; -. DR GO; GO:0009005; F:signal peptidase II activity; IEA:HAMAP. DR HAMAP; MF_00161; -; 1. DR InterPro; IPR001872; Peptidase_A8. DR Pfam; PF01252; Peptidase_A8; 1. DR PRINTS; PR00781; LIPOSIGPTASE. DR ProDom; PD004304; Peptidase_A8; 1. DR TIGRFAMs; TIGR00077; lspA; 1. DR PROSITE; PS00855; SPASE_II; 1. PE 3: Inferred from homology; KW Aspartyl protease; Complete proteome; Hydrolase; Membrane; Protease; KW Transmembrane. FT CHAIN 1 182 Lipoprotein signal peptidase. FT /FTId=PRO_0000289400. FT TRANSMEM 21 41 Potential. FT TRANSMEM 74 94 Potential. FT TRANSMEM 98 118 Potential. FT TRANSMEM 146 166 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 //