ID L8P845_STRVR Unreviewed; 228 AA.
AC L8P845;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=STVIR_5282 {ECO:0000313|EMBL:ELS53756.1};
OS Streptomyces viridochromogenes Tue57.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160705 {ECO:0000313|EMBL:ELS53756.1, ECO:0000313|Proteomes:UP000011205};
RN [1] {ECO:0000313|EMBL:ELS53756.1, ECO:0000313|Proteomes:UP000011205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue57 {ECO:0000313|EMBL:ELS53756.1,
RC ECO:0000313|Proteomes:UP000011205};
RX PubMed=23788550;
RA Gruning B.A., Erxleben A., Hahnlein A., Gunther S.;
RT "Draft Genome Sequence of Streptomyces viridochromogenes Strain Tu57,
RT Producer of Avilamycin.";
RL Genome Announc. 1:E00384-13(2013).
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: 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:ELS53756.1}.
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DR EMBL; AMLP01000157; ELS53756.1; -; Genomic_DNA.
DR AlphaFoldDB; L8P845; -.
DR PATRIC; fig|1160705.3.peg.5224; -.
DR Proteomes; UP000011205; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 185..210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 32..177
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 228 AA; 23825 MW; 60C68E00AB6F4FD1 CRC64;
MSGKGRGLAI AAVVVGLVGL SLGLGGVAYA RQAFGGSVVS SESMTPTYGP GDRVVFERVD
GSEVRRGDVV VFSAPDRYGF EGLVMERVIG VGGDHVVCCT GEGADTRVTV NGKPLQEPYV
KNAEASRGFG MASYDVRVPE GRLFMLGDHR ANARDSRAFL DDRGGTLPKS VIRGRVVEDY
TVPAVLGTAM MLGVVLTLVG VGLGIAAVVV RRKARALVPP PPPWAARV
//
