ID D7C8N0_STRBB Unreviewed; 294 AA.
AC D7C8N0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative serine protease {ECO:0000313|EMBL:ADI06419.1};
GN OrderedLocusNames=SBI_03298 {ECO:0000313|EMBL:ADI06419.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI06419.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI06419.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI06419.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP002047; ADI06419.1; -; Genomic_DNA.
DR RefSeq; WP_014175896.1; NC_016582.1.
DR AlphaFoldDB; D7C8N0; -.
DR STRING; 749414.SBI_03298; -.
DR MEROPS; S01.102; -.
DR KEGG; sbh:SBI_03298; -.
DR PATRIC; fig|749414.3.peg.3418; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_006842_7_0_11; -.
DR Proteomes; UP000000377; Chromosome.
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:ADI06419.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..294
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003093577"
FT DOMAIN 36..287
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 294 AA; 30404 MW; 96299DF192F6C950 CRC64;
MRRSLSALFA PLAAPLVTAL AMLAILPPPA TADRTVVGGH PAHTELAPWA VALASRERFG
GARSGQFCGG VVVGPTTVLT AAHCLSREVL GVDWWEVGDL RVIIGRDDLR GSGGVEMAPL
RAWVNPAYEQ VGRSGDVAVL TLAQPLPRIY GIAMAADGDL AYQPGARAAV YGWGDTRGNG
SYASTLRASR VRVLPDEACE EAYPGNAEGE YRSESMMCAG LPDGGRDACQ GDSGGPLVAR
GKLVGLVSWG SGCAEAGRPG VYTRISSVLS LATAAEADRE AAAEADWATA SDVE
//
