LSPA_PARPJ
ID LSPA_PARPJ Reviewed; 172 AA.
AC B2T6I8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Bphyt_3160;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD17552.1; -; Genomic_DNA.
DR RefSeq; WP_012434124.1; NC_010681.1.
DR AlphaFoldDB; B2T6I8; -.
DR SMR; B2T6I8; -.
DR STRING; 398527.Bphyt_3160; -.
DR EnsemblBacteria; ACD17552; ACD17552; Bphyt_3160.
DR KEGG; bpy:Bphyt_3160; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_4_0_4; -.
DR OMA; NRWYFPA; -.
DR OrthoDB; 1575081at2; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000001739; Chromosome 1.
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..172
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_1000097240"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 132
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 150
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 172 AA; 18764 MW; B74314269336A4C7 CRC64;
MARTMSKTAP KTSAANGSLA PWLGVALIVI LFDQLTKIAV QKVFAYGVAH EVTSFFNLIL
VYNRGAAFSF LAMAGGWQRW AFTALGVVAA LVICYLLKRH GGQKMFCTAL ALILGGALGN
VIDRLAYGHV IDFLDFHLRT WHWPAFNLAD SAITVGAVLL VLDELRRVRG SR
