ID A0A101NQX4_9ACTN Unreviewed; 648 AA.
AC A0A101NQX4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KUM97542.1};
GN ORFNames=AQI88_06300 {ECO:0000313|EMBL:KUM97542.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM97542.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM97542.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM97542.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KUM97542.1}.
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DR EMBL; LMWL01000009; KUM97542.1; -; Genomic_DNA.
DR RefSeq; WP_066993137.1; NZ_KQ948016.1.
DR AlphaFoldDB; A0A101NQX4; -.
DR STRING; 67285.AQI88_06300; -.
DR OrthoDB; 3480681at2; -.
DR Proteomes; UP000054241; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|EMBL:KUM97542.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KUM97542.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..648
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007101834"
FT DOMAIN 239..648
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 648 AA; 66621 MW; BF5087BA020A1758 CRC64;
MRSNRAKVRA GVSMAATLPM IAGALALGIP AAHAADTPAR DALAGTKPAW ATAKADKGAT
ADNAQVKARV YLAGKNAAGL AAYAKAVSDP SSAQYGKYLS AKKAQARFGA TKAQVAAVKS
WLKSAGLQVT EVTAHYVAVT GDVSAAEKAF GTQLHNFTKG GKTYRAPAKT ASAPAGLKGA
VLTVTGLDNA PHKSTHDDQL PQPDAVFKNS GPFSSYYGSN TATTLPDAYG QKIPYAIKGY
TGKQLRAAYG AGTYTGKNVR IAITDAYASP TIAFDAGTYA LKHGDAAWKT GQLHQVLPNN
YTKTKECGAA GWYGEETLDV QAVHAVAPDA DVTYVGAASC YDDDLLASLS KVVDNHLADI
VSNSWGDIEA NQTPDLAAAY DQVFQLGAVQ GIGFYFSSGD DGDQVAKSGT KQVDTPANSA
WVTAVGGTSL AVGKGDTYQW ETGWGTQKAT LSADGKSWTN FPGAFTSGAG GGTSKNVPQP
YYQKGVVPDS LAKANSADGN RVVPDIAAIA DPNTGFLVGQ TQTFPDGSLQ YSEYRIGGTS
LAAPVIAAVQ ALAQEARGGK AIGFANPTIY TKYGKKGVYH DVTDNPTGSG LAVARIDFVN
GLNASGGLAT SVRSLGKDSS LSAVKGYDDV TGVGSPADGY VASYAKKH
//
