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Database: UniProt
Entry: A0A101SL58_9ACTN
LinkDB: A0A101SL58_9ACTN
Original site: A0A101SL58_9ACTN 
ID   A0A101SL58_9ACTN        Unreviewed;       593 AA.
AC   A0A101SL58;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:KUN75722.1};
GN   ORFNames=AQJ64_41375 {ECO:0000313|EMBL:KUN75722.1};
OS   Streptomyces griseoruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN75722.1, ECO:0000313|Proteomes:UP000052982};
RN   [1] {ECO:0000313|EMBL:KUN75722.1, ECO:0000313|Proteomes:UP000052982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN75722.1,
RC   ECO:0000313|Proteomes:UP000052982};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT   for the species Streptomyces griseoruber.";
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:KUN75722.1}.
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DR   EMBL; LMWW01000074; KUN75722.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101SL58; -.
DR   STRING; 1943.AQJ64_41375; -.
DR   OrthoDB; 1496095at2; -.
DR   Proteomes; UP000052982; 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; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR028994; Integrin_alpha_N.
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; PF13517; FG-GAP_3; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 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:KUN75722.1};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..593
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007106329"
FT   DOMAIN          80..399
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          51..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  61579 MW;  660764733D06A571 CRC64;
     MRIALPVAAA GLAAAVAGVF VTTSAGAATA APTPVRSTPS TSEIEARLST ALAGDDTAGE
     TSKSSLGASS SSSTSVDPKI IGGSTTTITT APYMAQLWYG DNRGTSTTSD DIGFFCGGAV
     VAPTKILTAA HCVAGYNWKA HGVVVTGTAQ LLSEDSSGNP DLHGGNPSGV WRQWNHPSYD
     DNTIDNDLAV LTLPNPVKAT PIPMTTAGDT ASYTGAAAKT AQVFGWGRTS STSQDISDTL
     KTATLPIQSD ATCSAEYGSD FIAGHMVCAG EPATGSDTGT TSACNGDSGG PLVVGGKVVG
     VVSWGVKDCV AAGAYSVFTK LTTYVAAAYP RIDDTNLSGD HKADLFVRNS STKTGYEIDS
     KGTSLASRLS WGSHSAWNLV LQTDLDRDGY TDFIRRRASD GDLYWRHCVF PSNGTTCTWT
     NTLVGDNWKS RLAVVVPGDV TGDKLPDLLS VDSAGVLWIY PGKGNGRFAT RVKVSTGWNQ
     YNVVRGHGDL SNDGRADLLA RNKSTGAVYL YKGTGKAGTG AFSARVKVRT WSGTTYNAFD
     AVGDVNGDGK ADFLARTPGG TLYLYKGTGK ATSEIFATRV SLGTSFKQYD LFG
//
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