ID A0A1D8G736_9ACTN Unreviewed; 313 AA.
AC A0A1D8G736;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 Name=lepB_3 {ECO:0000313|EMBL:AOT61275.1};
GN ORFNames=A4G23_04158 {ECO:0000313|EMBL:AOT61275.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT61275.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT61275.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT61275.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-2016) 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|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}.
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DR EMBL; CP017316; AOT61275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8G736; -.
DR STRING; 285473.A4G23_04158; -.
DR KEGG; srn:A4G23_04158; -.
DR PATRIC; fig|285473.5.peg.4362; -.
DR Proteomes; UP000095349; 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; 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; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:AOT61275.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000095349};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 274..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 64..255
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 313 AA; 32980 MW; 730C3CC822EA0024 CRC64;
MTESAAVRGG APHGARSAEN TEGDTVDNDQ TVGGGGNGGG RDGGEGGDGD GGEGRPARQR
SFWKELPLLV GIALVLALLI KTFLVQAFSI PSESMMDTLK RGDRVLVDKL TPWFGSEPER
GEVVVFEDPG GWLNEPAPEP NPLQRFLSFI GLMPAADQQN LIKRVIAVGG DTVECKKGGK
VHVNGKALDE TSYLYPGSTP CDDEPFGPVK VPDGRIWVMG DNRQNSLDSR YHQELPGDGT
VSNEEVVGRA VVVAWPVGRW STLPVPDTFD QPGLSAAAAA AAGPGALGLA GAVPLVLWRR
RRLAAREEAG ARG
//
