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
//