ID Q6I695_STRGR Unreviewed; 255 AA.
AC Q6I695;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:BAD24662.1};
DE EC=3.4.21.4 {ECO:0000313|EMBL:SQA25082.1};
GN Name=sprU {ECO:0000313|EMBL:BAD24662.1};
GN ORFNames=NCTC13033_04830 {ECO:0000313|EMBL:SQA25082.1};
OS Streptomyces griseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1911 {ECO:0000313|EMBL:BAD24662.1};
RN [1] {ECO:0000313|EMBL:BAD24662.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15601713; DOI=10.1128/JB.187.1.286-295.2005;
RA Kato J.Y., Chi W.J., Ohnishi Y., Hong S.K., Horinouchi S.;
RT "Transcriptional control by A-factor of two trypsin genes in Streptomyces
RT griseus.";
RL J. Bacteriol. 187:286-295(2005).
RN [2] {ECO:0000313|EMBL:SQA25082.1, ECO:0000313|Proteomes:UP000251334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13033 {ECO:0000313|EMBL:SQA25082.1,
RC ECO:0000313|Proteomes:UP000251334};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; AB182576; BAD24662.1; -; Genomic_DNA.
DR EMBL; UAVD01000032; SQA25082.1; -; Genomic_DNA.
DR RefSeq; WP_012381357.1; NZ_UAVD01000032.1.
DR AlphaFoldDB; Q6I695; -.
DR MEROPS; S01.101; -.
DR GeneID; 6214424; -.
DR OMA; HEAEVHY; -.
DR OrthoDB; 1496095at2; -.
DR Proteomes; UP000251334; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 2.
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, ECO:0000313|EMBL:SQA25082.1};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..255
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033705429"
FT DOMAIN 34..253
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 255 AA; 26210 MW; C1D398F4AE930CF8 CRC64;
MKLLSVLKRC SVGIAAVALA TVSLQPASAA PQPIVGGERA AQGEFPFMVR LSMGCGGALY
AQDIVLTAAH CVDGSGDDTS ITVTGGVADL QSPDAVEVQS TKVLQAPGYN GTGKDWALIK
LAQPIDQPTL KIATDGAYDE GTFTVAGWGA DKEGGSQQRH LLKADVPFVT DADCQGAYGN
LVADEELCAG LLDTGGVDSC QGDSGGPMFR KDDADEWVQV GIVSWGQGCA RPNYPGVYTQ
VSHFAGDIAS AADSL
//
