ID A0A1P8WBU5_9PLAN Unreviewed; 191 AA. AC A0A1P8WBU5; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 28-MAR-2018, entry version 7. DE RecName: Full=Lipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161}; DE EC=3.4.23.36 {ECO:0000256|HAMAP-Rule:MF_00161}; DE AltName: Full=Prolipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161}; DE AltName: Full=Signal peptidase II {ECO:0000256|HAMAP-Rule:MF_00161}; DE Short=SPase II {ECO:0000256|HAMAP-Rule:MF_00161}; GN Name=lspA {ECO:0000256|HAMAP-Rule:MF_00161}; GN ORFNames=Fuma_01092 {ECO:0000313|EMBL:APZ91504.1}; OS Fuerstia marisgermanicae. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Fuerstia. OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ91504.1, ECO:0000313|Proteomes:UP000187735}; RN [1] {ECO:0000313|EMBL:APZ91504.1, ECO:0000313|Proteomes:UP000187735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH11 {ECO:0000313|EMBL:APZ91504.1, RC ECO:0000313|Proteomes:UP000187735}; RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079; RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., RA Rast P., Borchert D., Glockner I., Freese H.M., Klenk H.P., RA Overmann J., Kaster A.K., Rohde M., Wiegand S., Jogler C.; RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of RT the Phylum Planctomycetes from the German Wadden Sea."; RL Front. Microbiol. 7:2079-2079(2016). CC -!- FUNCTION: This protein specifically catalyzes the removal of CC signal peptides from prolipoproteins. {ECO:0000256|HAMAP- CC Rule:MF_00161, ECO:0000256|SAAS:SAAS00395969}. 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:0000256|HAMAP-Rule:MF_00161, CC ECO:0000256|SAAS:SAAS00396003}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). {ECO:0000256|HAMAP-Rule:MF_00161, CC ECO:0000256|SAAS:SAAS00396035}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00161}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00161}. CC -!- SIMILARITY: Belongs to the peptidase A8 family. CC {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU004181, CC ECO:0000256|SAAS:SAAS00581686}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|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; CP017641; APZ91504.1; -; Genomic_DNA. DR RefSeq; WP_077023252.1; NZ_CP017641.1. DR KEGG; fmr:Fuma_01092; -. DR KO; K03101; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000187735; 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 PROSITE; PS00855; SPASE_II; 1. PE 3: Inferred from homology; KW Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112503}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112556}; KW Complete proteome {ECO:0000313|Proteomes:UP000187735}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112525}; KW Lipoprotein {ECO:0000313|EMBL:APZ91504.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112491}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112585}; KW Reference proteome {ECO:0000313|Proteomes:UP000187735}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112497}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00112465}. FT TRANSMEM 69 89 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00161}. FT TRANSMEM 96 115 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00161}. FT ACT_SITE 116 116 {ECO:0000256|HAMAP-Rule:MF_00161}. FT ACT_SITE 161 161 {ECO:0000256|HAMAP-Rule:MF_00161}. SQ SEQUENCE 191 AA; 20951 MW; 1C70D9CA104CB151 CRC64; MNRLPRNRAV VFGIITASML AVDLWSKTAA FTAFPLRNGG PWLIDSTAVR FRFFTSLNEG ALWGFGQGFA WAFALLSVAA FVGVLYWLFV MKAAESLWLT ISLAFVSAGT LGNLYDRLGL HGIRLPGQDQ PIQAVRDFFH FQFGGTVQNP GLDWAIFNVA DICLVCGAGM LMIQSLFAPP EPTTQPVRTE S //