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Database: UniProt
Entry: A0A136PSI5_9ACTN
LinkDB: A0A136PSI5_9ACTN
Original site: A0A136PSI5_9ACTN 
ID   A0A136PSI5_9ACTN        Unreviewed;       210 AA.
AC   A0A136PSI5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=AWW66_13765 {ECO:0000313|EMBL:KXK61378.1};
OS   Micromonospora rosaria.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK61378.1, ECO:0000313|Proteomes:UP000070620};
RN   [1] {ECO:0000313|EMBL:KXK61378.1, ECO:0000313|Proteomes:UP000070620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 803 {ECO:0000313|EMBL:KXK61378.1,
RC   ECO:0000313|Proteomes:UP000070620};
RA   Yang H., He X., Zhu D.;
RT   "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT   which can produce antibacterial substance rosamicin.";
RL   Submitted (JAN-2016) 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}.
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:KXK61378.1}.
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DR   EMBL; LRQV01000042; KXK61378.1; -; Genomic_DNA.
DR   RefSeq; WP_067365250.1; NZ_LRQV01000042.1.
DR   AlphaFoldDB; A0A136PSI5; -.
DR   OrthoDB; 4308908at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000070620; 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   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:UP000070620};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        83..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        148..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   REGION          181..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..195
FT                   /note="Basic and acidic residues"
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   210 AA;  22230 MW;  72CB5DD7B3C02190 CRC64;
     MSAAPPAGSG RAEPGGGRAR PRVVAILFGL ALFLLVADQL LKDVALAGLE DRDEPVRLLG
     GAVYLTLVRN SGAAWSIGSG YTWVFPMITT GVVAWICWMA LRLRSLPWAI SLGLVLGGAL
     GNLGDRIFRA PGHFVGHVVD MVSLFDPYGR IIPVFNLADS SLVCGVILAV LLELTGRQRD
     GTRLADDKDP DADGVTASSP DDPAEQRERA
//
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