ID A0A101QU48_9ACTN Unreviewed; 594 AA.
AC A0A101QU48;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KUN36048.1};
GN ORFNames=AQJ30_22805 {ECO:0000313|EMBL:KUN36048.1};
OS Streptomyces longwoodensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN36048.1, ECO:0000313|Proteomes:UP000053271};
RN [1] {ECO:0000313|EMBL:KUN36048.1, ECO:0000313|Proteomes:UP000053271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN36048.1,
RC ECO:0000313|Proteomes:UP000053271};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT for the species Streptomyces longwoodensis.";
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:KUN36048.1}.
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DR EMBL; LMWS01000028; KUN36048.1; -; Genomic_DNA.
DR RefSeq; WP_067237124.1; NZ_KQ948556.1.
DR AlphaFoldDB; A0A101QU48; -.
DR STRING; 68231.AQJ30_22805; -.
DR Proteomes; UP000053271; 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:KUN36048.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053271};
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..594
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007104213"
FT DOMAIN 81..338
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 52..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 62001 MW; AC4E4B667DFB19D5 CRC64;
MRIALPVAAA GLAAAVAGVL LTSSAQAAET PPKPTVSAPS QAELEKRLAV AVAGDDTPGH
TGKEALSGST GTSTRTADPK IIGGTATSIT SAPWMAQLWY GDDRGTATTA DDIGFFCGGV
VVAPTKILTA AHCVRDEYNK NYSWYAHGTV ITGTAQLPTV DSNGQITDLH GGSYSGVWRQ
WNHPSYSPAT INNDIAVLTL PNPVKATPIR MTTATDTASY AAGTPATLFG WGRTSSTTQD
ISDVLKTATL PIQSDTTCAG AYGADFVKGH MVCAGNPATG SDEGTTSACN GDSGGPLIVK
GRIVGVVSWG VEDCVASGAY SVFTKVSSYV GAAYPRVEDT NLNGDHLADL FVRNASTKTA
YEIDSKGTSL AARTSWGNWN GYNLIVQTDL DRDGYQDLIV RRSSDGDVFW EHYVPATDSW
TTKLIGDNWK TRLNIVAPGD MTGDYLPDLL AVDSTGALWL YAGKGNGGFA APLKVGAGFN
NFNLVRGHGD FNGDGNADLL ARNKSTGAVY LYRSKGVAST ALWQPALKVA TWTSTTYNAL
VTVGDLNSDG KADLLARTPG GTLYLYKGTG ANTTASFGTR VSLGTGFQQY DLLG
//
