LSPA_PSESM
ID LSPA_PSESM Reviewed; 173 AA.
AC Q889E3;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PSPTO_0807;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54349.1; -; Genomic_DNA.
DR RefSeq; NP_790654.1; NC_004578.1.
DR RefSeq; WP_005769261.1; NC_004578.1.
DR AlphaFoldDB; Q889E3; -.
DR SMR; Q889E3; -.
DR STRING; 223283.PSPTO_0807; -.
DR EnsemblBacteria; AAO54349; AAO54349; PSPTO_0807.
DR GeneID; 1182432; -.
DR KEGG; pst:PSPTO_0807; -.
DR PATRIC; fig|223283.9.peg.820; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_4_0_6; -.
DR OMA; NRWYFPA; -.
DR OrthoDB; 1575081at2; -.
DR PhylomeDB; Q889E3; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000002515; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..173
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_0000178805"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 128
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 173 AA; 19320 MW; 6F4A124CC4673EAD CRC64;
MPDATLSNTS LGRLAWLWLT VLIVAVDQVS KYYFENALSL YQQIIVIPDY FSWTLAYNTG
AAFSFLADGA GWQRWLFALI AVVVSAVLVV WLKRLGRDDT WLAIALALVL GGALGNLYDR
VVLGHVIDFI LVHWQNRWYF PAFNVADSAI TVGAIMLALD MFKSKKTGET VND
