ID   A0A2G2L3P4_HALSX        Unreviewed;       165 AA.
AC   A0A2G2L3P4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   10-APR-2019, entry version 8.
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=COA87_07075 {ECO:0000313|EMBL:PHS17412.1};
OS   Halomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1486246 {ECO:0000313|EMBL:PHS17412.1};
RN   [1] {ECO:0000313|EMBL:PHS17412.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NORP57 {ECO:0000313|EMBL:PHS17412.1};
RX   PubMed=29099490; DOI=10.1038/ismej.2017.187;
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy
RT   inhabits the cold, oxic subseafloor aquifer.";
RL   ISME J. 12:1-16(2018).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins. {ECO:0000256|HAMAP-
CC       Rule:MF_00161, ECO:0000256|RuleBase:RU000594,
CC       ECO:0000256|SAAS:SAAS00395969}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of signal peptides from bacterial membrane
CC         prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-
CC         (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably
CC         Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small,
CC         neutral side chains.; EC=3.4.23.36; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00161, ECO:0000256|RuleBase:RU000594,
CC         ECO:0000256|SAAS:SAAS01126194};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage). {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|SAAS:SAAS00396035}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU004181,
CC       ECO:0000256|SAAS:SAAS00581686}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PHS17412.1}.
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DR   EMBL; NVVS01000041; PHS17412.1; -; Genomic_DNA.
DR   UniPathway; UPA00665; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695; PTHR33695; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   TIGRFAMs; TIGR00077; lspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112503};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112556};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112525};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112491};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112585};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112497};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112465}.
FT   TRANSMEM      6     25       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     62     82       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     91    108       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    128    148       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   ACT_SITE    109    109       {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    136    136       {ECO:0000256|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   165 AA;  18277 MW;  49A380C00172D72A CRC64;
     MQRPLRWLWL AVAVIVLDLA TKYVASSQLG YAQPVEVLPF FNLTLLHNTG AAFSFLATHP
     GWQRWFFALI AIGASVALTV WLSRIKNDEK LLAIALPLII GGALGNLYDR LVHGYVVDFL
     SFHVAGLYYP AFNVADIAIT LGAVALIWES IMGERRRKKA ANTSH
//