ID S4A672_9ACTN Unreviewed; 258 AA.
AC S4A672;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=STRAU_0662 {ECO:0000313|EMBL:EPH46270.1};
OS Streptomyces aurantiacus JA 4570.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH46270.1, ECO:0000313|Proteomes:UP000014629};
RN [1] {ECO:0000313|EMBL:EPH46270.1, ECO:0000313|Proteomes:UP000014629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH46270.1,
RC ECO:0000313|Proteomes:UP000014629};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT Setomimycin.";
RL Submitted (FEB-2013) 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:EPH46270.1}.
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DR EMBL; AOPZ01000021; EPH46270.1; -; Genomic_DNA.
DR RefSeq; WP_016638795.1; NZ_AOPZ01000021.1.
DR AlphaFoldDB; S4A672; -.
DR PATRIC; fig|1286094.4.peg.645; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000014629; 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:UP000014629};
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 206..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 27..181
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 237..258
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 258 AA; 26317 MW; B5C6DA866AB58A03 CRC64;
MSTTRRTDEG HGRLGSTLSG VAVALGCVLF LGGFVWGALV YQPYTVPTGS MTPTIGAGDR
VLAQRIDGDD VRRGDVIVFR QQTWGDLPMV KRVVGVGGDK VACCTGGKLT VNGKQIDEPY
LPKGGGASAT GIKETAVPEG RLFLLGDERS GSMDSSVHLQ DADGGTVPRS AVKGRVDAVA
WPLDGMLDRT TAFDDLPGGT SDPGPLRLQL AAVVAGAVLI LGGAAYGPIA KRARRRAGQT
GNAGGGRSSG TTEAAGVG
//
