GenomeNet

Database: UniProt
Entry: A0A0S7Y9B5_9BACT
LinkDB: A0A0S7Y9B5_9BACT
Original site: A0A0S7Y9B5_9BACT 
ID   A0A0S7Y9B5_9BACT        Unreviewed;       180 AA.
AC   A0A0S7Y9B5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   ORFNames=AMJ50_02745 {ECO:0000313|EMBL:KPJ71254.1};
OS   Parcubacteria bacterium DG_74_3.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1703767 {ECO:0000313|EMBL:KPJ71254.1, ECO:0000313|Proteomes:UP000051833};
RN   [1] {ECO:0000313|EMBL:KPJ71254.1, ECO:0000313|Proteomes:UP000051833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_74_3 {ECO:0000313|EMBL:KPJ71254.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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|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|RuleBase:RU362042}.
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:KPJ71254.1}.
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; LJNG01000014; KPJ71254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7Y9B5; -.
DR   STRING; 1703767.AMJ50_02745; -.
DR   Proteomes; UP000051833; Unassembled WGS sequence.
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   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042}.
FT   DOMAIN          42..179
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   180 AA;  20444 MW;  448FAB398D256CED CRC64;
     MFLIISGFLV FIFFFYFYLN KLDPSLENLN KECVIQTEKK IVQGNSLNGL IESGEVVEIL
     FDYYNCNEVE REDVVLLNYP GFEKPIIKIV KGVSGDRFQL KETEQGWHVL INGNILQNSE
     GIPYLLNEKR VGMLKLYEKD YRGIIPDNTL LLLGNLPSGS IDSTIFGLVD KSGILGKAIR
//
DBGET integrated database retrieval system