ID A0A1V2REU2_9ACTN Unreviewed; 398 AA.
AC A0A1V2REU2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=STBA_16360 {ECO:0000313|EMBL:ONK10911.1};
OS Streptomyces sp. MP131-18.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK10911.1, ECO:0000313|Proteomes:UP000189065};
RN [1] {ECO:0000313|EMBL:ONK10911.1, ECO:0000313|Proteomes:UP000189065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP131-18 {ECO:0000313|EMBL:ONK10911.1,
RC ECO:0000313|Proteomes:UP000189065};
RA Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT "New natural products identified by combined genomics-metabolomics
RT profiling of marine Streptomyces sp. MP131-18.";
RL Submitted (JUN-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:ONK10911.1}.
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DR EMBL; LZNS01000001; ONK10911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2REU2; -.
DR STRING; 1857892.STBA_16360; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000189065; 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, ECO:0000313|EMBL:ONK10911.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000189065};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 70..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 70..267
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 177
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 398 AA; 43049 MW; 77D696195305D423 CRC64;
MGERGKPRSG RRRNGGPEGA GDGAYPAGAE QPAGEEPRPT LRGPGEGRAD RRRAARRIRR
RRRLRATREI PILIGTALLI ALVLKTFLVQ AFVIPSGSME ETIRVDDRVL VDKLTPWFGW
EPSRGDVVVF TDPGGWLETE QAGDTDEDEG PFGIRHVQAA LTWIGLLPSD DDQDLIKRVI
GVGGDTVVCC DADGRITVNG TPLDEPYLYP GNPPSQIEFE VTVPDGRVFV MGDHRSNSAD
SRYHLDEEGQ GTVPVDLVVG RAVVIAWPFG HWQRLGGTEA FADVPDPAAG AVDARATGGD
NAVRTDNQIA RLPIPAELPL VMGVVGLLRK PGGPERSVRS ECGGCSGGCA IRFGRRPGEP
PAASGWRGVR RRSPRCAGRL RGRLRRRRSG RGRDRGEP
//
