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Database: UniProt
Entry: A0A3Q8V5B2_9ACTN
LinkDB: A0A3Q8V5B2_9ACTN
Original site: A0A3Q8V5B2_9ACTN 
ID   A0A3Q8V5B2_9ACTN        Unreviewed;       239 AA.
AC   A0A3Q8V5B2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   Name=lepB {ECO:0000313|EMBL:AZM55797.1};
GN   ORFNames=DMA15_27085 {ECO:0000313|EMBL:AZM55797.1};
OS   Streptomyces sp. WAC 01529.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203205 {ECO:0000313|EMBL:AZM55797.1, ECO:0000313|Proteomes:UP000269043};
RN   [1] {ECO:0000313|EMBL:AZM55797.1, ECO:0000313|Proteomes:UP000269043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01529 {ECO:0000313|EMBL:AZM55797.1,
RC   ECO:0000313|Proteomes:UP000269043};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; CP029617; AZM55797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8V5B2; -.
DR   OrthoDB; 9815782at2; -.
DR   Proteomes; UP000269043; 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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362042};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          54..214
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   239 AA;  25700 MW;  9426616C8A0939C6 CRC64;
     MDTEAQHTER DRSSAPSDSG DVPHVTEASE ETEERSRSVF MSLLARLPGG GLTLTFLLCV
     GALLLVSAFV VQPFQIPSGS MEPAFRVGDR VLVNKLAYRF GSEPQRGDAV VFDGSGYFGD
     ADYIKRVVGT GGDRVVCCEG GGIKVNGEPV DEPYLYPGDR PSTVPFDVVV PEGSLFLLGD
     HRSDSRDSRD HLGEPGGGMI PVEEVIGRAD WIAWPIGHWT SLERPDGYAR VPEPGGTHG
//
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