ID I0V6C8_9PSEU Unreviewed; 222 AA.
AC I0V6C8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ORFNames=SacxiDRAFT_3480 {ECO:0000313|EMBL:EID55681.1};
OS Saccharomonospora xinjiangensis XJ-54.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882086 {ECO:0000313|EMBL:EID55681.1, ECO:0000313|Proteomes:UP000004691};
RN [1] {ECO:0000313|EMBL:EID55681.1, ECO:0000313|Proteomes:UP000004691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XJ-54 {ECO:0000313|EMBL:EID55681.1,
RC ECO:0000313|Proteomes:UP000004691};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "Improved High-Quality Draft sequence of Saccharomonospora xinjiangensis
RT XJ-54.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; JH636049; EID55681.1; -; Genomic_DNA.
DR RefSeq; WP_006239862.1; NZ_JH636049.1.
DR AlphaFoldDB; I0V6C8; -.
DR STRING; 882086.SacxiDRAFT_3480; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_2_2_11; -.
DR OrthoDB; 4308908at2; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000004691; Unassembled WGS sequence.
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 Lipoprotein {ECO:0000313|EMBL:EID55681.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 154..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 159
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 222 AA; 23525 MW; 5EE766086304E784 CRC64;
MNTEQQPDPS HTEEPQQDPR PTRKVGLLAL VALLAYAVDV VTKVVVTATL EGEEPIRLLG
GAVYLQLLRN PYAAFGMDIG GTWILTVVAI AVVVGIVWFA RRLRSAGWAV GLGLVLAGAL
GNLTDRIFRA PGVFQGHVVD FISVFAPNGE FFPVFNAADS AITIGAGLVV LLTLLGRDYD
GSVIPRGRRA KGTEPDIDAG TDSDDSERGT DQDADGKGRS AE
//
