ID A0A1X0CT47_9MYCO Unreviewed; 167 AA.
AC A0A1X0CT47;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Lipoprotein signal peptidase {ECO:0000256|RuleBase:RU000594};
DE EC=3.4.23.36 {ECO:0000256|RuleBase:RU000594};
DE Flags: Fragment;
GN ORFNames=BST26_20475 {ECO:0000313|EMBL:ORA63268.1};
OS Mycolicibacterium insubricum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=444597 {ECO:0000313|EMBL:ORA63268.1, ECO:0000313|Proteomes:UP000192801};
RN [1] {ECO:0000313|EMBL:ORA63268.1, ECO:0000313|Proteomes:UP000192801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45130 {ECO:0000313|EMBL:ORA63268.1,
RC ECO:0000313|Proteomes:UP000192801};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC peptides from prolipoproteins. {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|RuleBase:RU000594};
CC -!- SIMILARITY: Belongs to the peptidase A8 family.
CC {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|RuleBase:RU004181}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORA63268.1}.
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DR EMBL; MVHS01000084; ORA63268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0CT47; -.
DR STRING; 444597.BST26_20475; -.
DR OrthoDB; 4308908at2; -.
DR Proteomes; UP000192801; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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,
KW ECO:0000256|RuleBase:RU000594};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000594};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU000594};
KW Reference proteome {ECO:0000313|Proteomes:UP000192801};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ORA63268.1"
SQ SEQUENCE 167 AA; 18046 MW; 87D48F3E43CEE557 CRC64;
PRPRPRRQVL LLLLVAAFVL AVDVATKVLA VKMLTPFQPV EIIGETVTWN LQRNSGAAFS
MFRGSTWVLT LIAAGVVIGI VWMGRRLVSK WWALGLGMIL GGALGNLGDR IFRAPAPLHG
QVVDFISIGW WPTFNVADSA VVGGAILLVA LSLFGVDYDT PARRADD
//
