ID A0A1P8WBU5_9PLAN Unreviewed; 191 AA. AC A0A1P8WBU5; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 03-AUG-2022, entry version 18. 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 Fuerstiella marisgermanici. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Fuerstiella. 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., Rast P., RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J., RA Kaster A.K., Rohde M., Wiegand S., Jogler C.; RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the RT Phylum Planctomycetes from the German Wadden Sea."; RL Front. Microbiol. 7:2079-2079(2016). CC -!- FUNCTION: This protein specifically catalyzes the removal of signal CC peptides from prolipoproteins. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00161}; CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide CC cleavage). {ECO:0000256|HAMAP-Rule:MF_00161}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00161}. CC -!- SIMILARITY: Belongs to the peptidase A8 family. CC {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|HAMAP-Rule:MF_00161, CC ECO:0000256|RuleBase:RU004181}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 STRING; 1891926.Fuma_01092; -. DR EnsemblBacteria; APZ91504; APZ91504; Fuma_01092. DR KEGG; fmr:Fuma_01092; -. DR OrthoDB; 1575081at2; -. 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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|ARBA:ARBA00022750, ECO:0000256|HAMAP- KW Rule:MF_00161}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00161}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00161}; KW Lipoprotein {ECO:0000313|EMBL:APZ91504.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00161}; KW Reference proteome {ECO:0000313|Proteomes:UP000187735}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}. FT TRANSMEM 69..89 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161" FT TRANSMEM 96..115 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161" FT ACT_SITE 137 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161" FT ACT_SITE 161 FT /evidence="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 //