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Database: UniProt
Entry: A0A1Q4VZ36_9ACTN
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Original site: A0A1Q4VZ36_9ACTN 
ID   A0A1Q4VZ36_9ACTN        Unreviewed;       196 AA.
AC   A0A1Q4VZ36;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=AMK13_28685 {ECO:0000313|EMBL:OKI03094.1};
OS   Streptomyces sp. CB02056.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI03094.1, ECO:0000313|Proteomes:UP000186379};
RN   [1] {ECO:0000313|EMBL:OKI03094.1, ECO:0000313|Proteomes:UP000186379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02056 {ECO:0000313|EMBL:OKI03094.1,
RC   ECO:0000313|Proteomes:UP000186379};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC       peptides from prolipoproteins. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00161};
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00161}.
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:OKI03094.1}.
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DR   EMBL; LIPD01000011; OKI03094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4VZ36; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000186379; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186379};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   TRANSMEM        80..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        142..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   REGION          175..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   196 AA;  21085 MW;  08544BEBA2421D74 CRC64;
     MTGLLRLRVA RGASLSGDTP RRLGTMTAVA IALLASDFIT KQIALTHFSG TDPTSTLGGL
     LKFTLVFNSG GAFSIGAGET WFFTTVKMLV IVLMLVVSPR IRTPLWAVSF GLVIAGAAGN
     LIDRLFRDPS PWEGRVVDWI QLPHWPVFNL ADCGVVCGSA LVMWASMRGI RLDGTRATEE
     PAEPDATERT AEVKNP
//
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