ID F5X200_STRPX Unreviewed; 157 AA.
AC F5X200;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
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 ECO:0000313|EMBL:BAK30309.1};
GN OrderedLocusNames=SGPB_1261 {ECO:0000313|EMBL:BAK30309.1};
OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30309.1, ECO:0000313|Proteomes:UP000007946};
RN [1] {ECO:0000313|EMBL:BAK30309.1, ECO:0000313|Proteomes:UP000007946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC {ECO:0000313|Proteomes:UP000007946};
RX PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA Chang C.-H., Hsu M.-T.;
RT "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL PLoS ONE 6:E20519-E20519(2011).
CC -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC peptides from prolipoproteins. {ECO:0000256|HAMAP-Rule:MF_00161,
CC ECO:0000256|RuleBase:RU000594}.
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 ECO:0000256|RuleBase:RU000594};
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}.
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DR EMBL; AP012054; BAK30309.1; -; Genomic_DNA.
DR RefSeq; WP_003065359.1; NC_015600.1.
DR AlphaFoldDB; F5X200; -.
DR STRING; 981540.SGPB_1261; -.
DR GeneID; 76468139; -.
DR KEGG; stb:SGPB_1261; -.
DR HOGENOM; CLU_083252_3_3_9; -.
DR OMA; NRWYFPA; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000007946; Chromosome.
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 NCBIfam; TIGR00077; lspA; 1.
DR PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161};
KW Protease {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU000594};
KW Reference proteome {ECO:0000313|Proteomes:UP000007946};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 133
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 157 AA; 17861 MW; 5C0FCCD9697E3E7C CRC64;
MKTLRKVYFP LAAVVLIVLD QLSKLWIVNH ITLDTIQECL PGIFSLTYLR NYGAAFSILQ
NQQWLFAVIT FAVVGAACYY FVKNINGQFW FLLGLILIIS GGLGNFIDRV RLGYVVDMIH
LDFMNFAVFN MADSYLTVGV VILFIALWKE EENGVNH
//