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Database: UniProt
Entry: A0A1Y1CF83_9BACT
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ID   A0A1Y1CF83_9BACT        Unreviewed;       462 AA.
AC   A0A1Y1CF83;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   ORFNames=ALGA_0584 {ECO:0000313|EMBL:BAX78974.1};
OS   Labilibaculum antarcticum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Labilibaculum.
OX   NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX78974.1, ECO:0000313|Proteomes:UP000218267};
RN   [1] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:BAX78974.1, ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|EMBL:BAX78974.1,
RC   ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 39:1-2(2018).
RN   [3] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT   psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL   Antonie Van Leeuwenhoek 113:349-355(2020).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU362042};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; AP018042; BAX78974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1CF83; -.
DR   KEGG; mbas:ALGA_0584; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000218267; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 2.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 2.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 2.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        12..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          64..268
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          395..439
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   462 AA;  53563 MW;  7BC2E9AB766E32C2 CRC64;
     MSSILRNKWF KFSIALIICL LMIIWIGNYW LILGLPILFD VYISKKVHWA FWKKKGVKKQ
     SATVEWVDAI IFAVIAATLI RMFFIEAYTI PTSSMEKSLL VGDYLFVSKV AYGPKIPNTP
     LSFPFAHHTM PLTKSTKSYL EWIQWPYKRL AGISEVKRND IVVFNFPAGD TIVVGAENPD
     YYSQLRSYST LFKEADMKKG RELQSDQEYT KMGRKYLSTQ NTIATRPVDK QENYIKRCVG
     IPGDTLLSID GQLFINGKKQ DLIEELQFIY EVRTNGSSIN PRKLEELNIA KADRNHNGSV
     YNLPLSTKKV EELKKLSNVV SIIRRNSSKG YPEDVFPFSS YYNWNRDNFG PLVIPKKGQT
     VSLNLETLPL YERAINAYEG NALRVQDSTI YINGEIATDF TFKMDYYWMM GDNRHMSADS
     RYWGYVPEDH IVGKASFLWL SLDKDKSSFN KIRWDRVFKW IH
//
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