ID D6EP52_STRLI Unreviewed; 285 AA.
AC D6EP52;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:EFD66269.2};
GN ORFNames=SSPG_01909 {ECO:0000313|EMBL:EFD66269.2};
OS Streptomyces lividans TK24.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD66269.2};
RN [1] {ECO:0000313|EMBL:EFD66269.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TK24 {ECO:0000313|EMBL:EFD66269.2};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces lividans strain TK24.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG657756; EFD66269.2; -; Genomic_DNA.
DR RefSeq; WP_003973201.1; NZ_GG657756.1.
DR AlphaFoldDB; D6EP52; -.
DR MEROPS; S01.102; -.
DR HOGENOM; CLU_006842_7_0_11; -.
DR Proteomes; UP000002769; 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:0000313|EMBL:EFD66269.2};
KW Protease {ECO:0000313|EMBL:EFD66269.2}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..285
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039640105"
SQ SEQUENCE 285 AA; 29071 MW; D230AAEABD6C0249 CRC64;
MRRLFARTLA RPLVLAAAAT AIPLGSAAPA AADSIVVGGF PVEVSDSPWT VALSSRDRFG
GTRAGQFCGG VAVGRTTVLT AAHCLGEEVL GSPPEQVDDL RVIAGRTDLL SDRGQEIPVR
SVWVNPEHDD GTNAGDFAVL TLSEALPAGS VIGMAAEGDP AYTPDTAALV YGWGDTSGAG
DYANGLHASR VRVLPDASCE RAYPGDDDGH YLPATMLCAG EEAGGRDACQ GDSGGPLVGR
GRLIGLVSWG SGCGRPGSPG VYTRVSSILR TLGWDGTAAQ QRGGV
//
