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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//