ID A0A0B5DA02_9ACTN Unreviewed; 646 AA.
AC A0A0B5DA02;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:AJE40413.1, ECO:0000313|EMBL:MBB4791443.1};
GN ORFNames=BJY54_002055 {ECO:0000313|EMBL:MBB4791443.1}, CP978_10745
GN {ECO:0000313|EMBL:QEV38978.1}, SNOD_10405
GN {ECO:0000313|EMBL:AJE40413.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE40413.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE40413.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE40413.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV38978.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV38978.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4791443.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4791443.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009313; AJE40413.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4791443.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV38978.1; -; Genomic_DNA.
DR RefSeq; WP_043439828.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_10405; -.
DR KEGG; snq:CP978_10745; -.
DR HOGENOM; CLU_012501_2_0_11; -.
DR OrthoDB; 3480681at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240,
KW ECO:0000313|EMBL:AJE40413.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..646
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041120321"
FT DOMAIN 239..646
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 36..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 540
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 646 AA; 66440 MW; 57DBED446C2123EB CRC64;
MRSNRATARA GVGLAATLPL LAGALAFGIP AAHAADDPGR DTLTGTKPAW ATATADRGAT
PKGTRISARV HLAGRDASGL AAYAKAVSDP ASPLYGKYLT PRQAQQRFGA SKAQVAAVTS
WLESAGLTIT DVTPRYIAVT GDASAAEKAF GAQLHNYAKG SRTYRAPSRT ASAPAGLKGA
VLTVTGLDNA PHKATHKDQL PPPDDVFKNA GPFSSYHGSN VATTLPSVQG SKIPYAVEGY
TGKQLRAAYG AGKRTGKGVR IAITDAYASP TIASDAATYA KKHGDAGYAK GQLSQVLPKK
YTRTEECGAA GWYGEETLDV EAAHAVAPGA DIVYVGAASC YDDDLLDSLG KIVDSRLADI
VSNSWGDIEA NETPDVAAAY DQVFMFGAVE GIGFYFSSGD DGDEVANTGT KQVDTPANSA
WVTAVGGTSL AVGKGDSYLW ETGWGTEKAS LSADGRSWAG FPGAFTSGAG GGTSRTVPQP
SYQKGVVPNS LAKANSSAGN RVVPDIAAIA DPNTGFKVGQ TQTFPDGSQR YDEYRIGGTS
LAAPVIAGVQ ALAQEAHGGK AIGFANPAIY ARYGSKVYHD VTDSPTHSTL AVARVDYLNG
YDATDGLATS VRSLGKDSSL SAVKGYDAVT GVGSPAPGYV ESWNRR
//
