ID A0A0C2B6T1_9ACTN Unreviewed; 252 AA.
AC A0A0C2B6T1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=QR77_30320 {ECO:0000313|EMBL:KIF76995.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF76995.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF76995.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF76995.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KIF76995.1}.
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DR EMBL; JTHL01000001; KIF76995.1; -; Genomic_DNA.
DR RefSeq; WP_040025192.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C2B6T1; -.
DR STRING; 1576605.QR77_30320; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000031584; 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 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 24..183
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 252 AA; 25868 MW; 2E029C26C947E210 CRC64;
MSGTGRTNDG RGGLGSALSG VAVAVGCVLF LGGFVWGAIA YQPYTVPTDS MTPTVKAGDR
VLAQRISGDD VRRGDVVVFQ DPDWGDMPMV KRVVGVGGDT VACCDAHGQL TVSGKAIPEP
YLGKSYSERA SESTFSSKVP TGQLFLLGDE RSDSLDSRVH IQDKSRGSVP RAEVKARVDA
VVWPLGSLIG RPNGFAALPG GVSSPGPLKL VVGAVVVGAV LILGGAAYGP IARRKPRTRR
PGRAGAGVSA GV
//
