ID A0A117PWL6_9ACTN Unreviewed; 263 AA.
AC A0A117PWL6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KUM95857.1};
GN ORFNames=AQI88_14645 {ECO:0000313|EMBL:KUM95857.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM95857.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM95857.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM95857.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:KUM95857.1}.
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DR EMBL; LMWL01000026; KUM95857.1; -; Genomic_DNA.
DR RefSeq; WP_066997879.1; NZ_KQ948020.1.
DR AlphaFoldDB; A0A117PWL6; -.
DR STRING; 67285.AQI88_14645; -.
DR OrthoDB; 1496095at2; -.
DR Proteomes; UP000054241; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:KUM95857.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..263
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007153695"
FT DOMAIN 38..262
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 263 AA; 26525 MW; 661668C732A99367 CRC64;
MFGLRRARQT AATLVATAAA AATALVASPT ATAAPQPIVG GTTTTTTAYP FMMQITDASG
NQFCGGTLVA AKKVVTAAHC MVGESAGNVR VVGGRTYLNG TNGTVSKVAK IWINPDYTDA
TNGHDVAVLT LSTAMSYTPA SYVSSSQTSV YAAGTTARIL GWGTTSENGS SSNQLRTATV
PVVADSSCKS SYGSDFVQTD MVCAGYTSGG TDTCQGDSGG PLLIGGVLAG ITSWGEGCAE
AGYPGVYSRL TTFSDLVTAQ VNS
//
