LSPA_BRUSI
ID LSPA_BRUSI Reviewed; 160 AA.
AC B0CIQ7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BSUIS_A0150;
OS Brucella suis (strain ATCC 23445 / NCTC 10510).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=470137;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23445 / NCTC 10510;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000911; ABY37253.1; -; Genomic_DNA.
DR RefSeq; WP_002965397.1; NC_010169.1.
DR AlphaFoldDB; B0CIQ7; -.
DR SMR; B0CIQ7; -.
DR EnsemblBacteria; ABY37253; ABY37253; BSUIS_A0150.
DR GeneID; 45123639; -.
DR GeneID; 55589940; -.
DR KEGG; bmt:BSUIS_A0150; -.
DR HOGENOM; CLU_083252_4_3_5; -.
DR OMA; NRWYFPA; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000008545; Chromosome I.
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..160
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_1000076919"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 160 AA; 18230 MW; D88410930B2A0B74 CRC64;
MKRHAVWSSL FVVILAVLID QGIKYLVESR MFYGQQIDLL PFLALFRTHN EGIAFSMLAW
LHDGGLIAIT LAVIAFVLYL WWTNAPERVF ARYGFALVIG GAIGNLIDRV MHGYVVDYVL
FHLPTWSFAV FNLADAFITI GAGLIILEEF LGWRRERISH
