LSPA_BLOPB
ID LSPA_BLOPB Reviewed; 165 AA.
AC Q493S2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BPEN_123;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00161}.
CC -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP-
CC Rule:MF_00161}.
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DR EMBL; CP000016; AAZ40763.1; -; Genomic_DNA.
DR RefSeq; WP_011282670.1; NC_007292.1.
DR AlphaFoldDB; Q493S2; -.
DR SMR; Q493S2; -.
DR STRING; 291272.BPEN_123; -.
DR EnsemblBacteria; AAZ40763; AAZ40763; BPEN_123.
DR KEGG; bpn:BPEN_123; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_4_0_6; -.
DR OMA; NRWYFPA; -.
DR BioCyc; CBLO291272:BPEN_RS00600-MON; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000007794; 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 TIGRFAMs; TIGR00077; lspA; 1.
DR PROSITE; PS00855; SPASE_II; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..165
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_1000076917"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 141
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 165 AA; 19343 MW; 0738296C201A6AAA CRC64;
MNNKYNYKNL KWLWLSILIM LLDIGTKYWV KTHFWIGEVL SVLPGINCYY VCNPGLAFGL
FTNASLYYRW LFVWIITLVI VAFIIALYKL IERPKCYSIS YSMVIGGALG NLLDRILYGA
VVDFIDVHIK NWHWPTFNVA DIAICIGITI VTIRFYYDFI KNNLY