GenomeNet

Database: UniProt
Entry: A0A0P0URA8_9GAMM
LinkDB: A0A0P0URA8_9GAMM
Original site: A0A0P0URA8_9GAMM 
ID   A0A0P0URA8_9GAMM        Unreviewed;       306 AA.
AC   A0A0P0URA8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   Name=lepB {ECO:0000313|EMBL:BAS67768.1};
GN   ORFNames=BSEPE_0775 {ECO:0000313|EMBL:BAS67768.1};
OS   endosymbiont of Bathymodiolus septemdierum str. Myojin knoll.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS67768.1, ECO:0000313|Proteomes:UP000067399};
RN   [1] {ECO:0000313|EMBL:BAS67768.1, ECO:0000313|Proteomes:UP000067399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67768.1,
RC   ECO:0000313|Proteomes:UP000067399};
RA   Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., Hashimoto J.;
RT   "Phylogenetic characterization of endosymbionts in three hydrothermal vent
RT   mussels: influence on host distributions.";
RL   Mar. Ecol. Prog. Ser. 208:147-155(2000).
RN   [2] {ECO:0000313|EMBL:BAS67768.1, ECO:0000313|Proteomes:UP000067399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67768.1,
RC   ECO:0000313|Proteomes:UP000067399};
RX   PubMed=26418631; DOI=10.1038/ismej.2015.176;
RA   Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S.,
RA   Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., Tamotsu H.,
RA   Hirano T., Maruyama T., Yoshida T.;
RT   "Heterogeneous composition of key metabolic gene clusters in a vent mussel
RT   symbiont population.";
RL   ISME J. 10:990-1001(2016).
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:RU003993};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, 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; AP013042; BAS67768.1; -; Genomic_DNA.
DR   RefSeq; WP_070104559.1; NZ_AP013042.1.
DR   AlphaFoldDB; A0A0P0URA8; -.
DR   STRING; 1303921.BSEPE_0775; -.
DR   KEGG; ebh:BSEPE_0775; -.
DR   OrthoDB; 9815782at2; -.
DR   Proteomes; UP000067399; 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; 1.
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; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:BAS67768.1};
KW   Membrane {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067399};
KW   Transmembrane {ECO:0000256|RuleBase:RU003993};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT   TRANSMEM        17..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   DOMAIN          79..277
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   306 AA;  34885 MW;  8A265BD9D5F14CA6 CRC64;
     MTIENASSFL AWDVSSYLAV FLIMAFIIVV TDHFFMGGSV VNAPTTKKSL LGKWLYFVCF
     LKLNKSKKYL HRSKIVQLSA EFYPMLLLIF ALRGFIVEPF RIPSNSMMPT FLTYDFLLVD
     KISYGIHLPI LNTELLDIGD PERGDVVVFR YPNYEKRSTY KGADFIKRVI GLPGDKIEYI
     NDQLTVNGEA VEYKKIGTYS GIEKGIEMTG YRHVRELLGD NPHDVLLHPR KNSRSVRLVV
     PQGHYFVMGD NRANSSDSRF WGFVPEKYII GRAFYIWAHG DIGGLFSSSP LKALKTFTFS
     RNGVID
//
DBGET integrated database retrieval system