ID A0A1A5P5W7_9ACTN Unreviewed; 364 AA.
AC A0A1A5P5W7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=A4U61_11170 {ECO:0000313|EMBL:OBQ50716.1};
OS Streptomyces sp. H-KF8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1727216 {ECO:0000313|EMBL:OBQ50716.1, ECO:0000313|Proteomes:UP000093719};
RN [1] {ECO:0000313|Proteomes:UP000093719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-KF8 {ECO:0000313|Proteomes:UP000093719};
RA Undabarrena A., Ugalde J.A., Seeger M., Camara B.;
RL Submitted (APR-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: 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:OBQ50716.1}.
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DR EMBL; LWAB01000010; OBQ50716.1; -; Genomic_DNA.
DR RefSeq; WP_065001777.1; NZ_LWAB01000010.1.
DR AlphaFoldDB; A0A1A5P5W7; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000093719; 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; 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000093719};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 56..253
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 162
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 364 AA; 39803 MW; C53DD9BCE0EBD286 CRC64;
MGNRGKPRGV PASASDNLLP TGARRAVSAS SGRSRADRRK LQQKVKRRRR RGAVKEIPLL
IGVAVLIALV LKTFLVQAFV IPSGSMEQTI QIGDRVLVDK LTPWFGSKPQ RGDVVVFKDP
GGWLQDEQPL PQKEDPVGVK QVKAGLTFIG LLPSENEKDL IKRVVGVGGD RVQCCDTQGR
VTVNGVPLEE GDYLFPGNAP STTPFDVTVP PGRLWVMGDH RSNSADSRAH QDTDYGGTVS
EEEVVGRAVV IAWPFGRWNT LDEPKAYASV SDSAPGSTAA DRLSHRVAPD DPNGMIRLPS
PAELPLVMGV VGLRRAWGRR RHRVRSWRGG CGGWRTVRSR RGGTPRAYRG ALRTGRGRRR
DLRE
//
