ID V6JV49_STRRC Unreviewed; 630 AA.
AC V6JV49;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:EST23697.1};
GN ORFNames=M878_32835 {ECO:0000313|EMBL:EST23697.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST23697.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST23697.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST23697.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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:EST23697.1}.
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DR EMBL; AWQX01000279; EST23697.1; -; Genomic_DNA.
DR AlphaFoldDB; V6JV49; -.
DR STRING; 1352936.M878_32835; -.
DR PATRIC; fig|1352936.5.peg.6839; -.
DR HOGENOM; CLU_012501_2_0_11; -.
DR Proteomes; UP000017984; Chromosome.
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:EST23697.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EST23697.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017984}.
FT DOMAIN 220..629
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 630 AA; 64697 MW; D444ECE2DD1D67DF CRC64;
MVAGALALGI PAAHAADSPA RNALKGTKPL WATAKADKGA TSDSAQINAR VYLAGKDAAG
LAAYAKAVSD PSSPLYGKYL SAKKAQAQFG ATKAQVSAVK SWLTSAGLKV TEVTQHYVAV
SGDVAAAEKA FGTQLHNYAK GSATYRAPAQ AASVPAALKD AVLTVTGLDN APHMANHDDT
LPPPDAVFKN AGPFSSYYGS KIASTLPDAY GQKVPYAIKG YTGKQLRAAY GAGTYTGKGV
RIAITDAYAS PTLAFDAGTY AAKNGDQAWK TSQLHQSLPD SYTRTDECKA AGWYGEETLD
VEAVHAVAPS ADVTYVGAAS CYDEDLLGSL SKVVDNHLAD IVSNSWGDVE ASQTPDLAAA
YDQVFQLGAV QGIGFYFSSG DNGDEVAHTK TKQVDTPANS AWVTAVGGTS LAVGKGDTYQ
WETGWGTEKA TLSADGKSWT NFPGAFTSGA GGGTSKTVAE PYYQKGVVPD ALAQANSASG
NRVVPDIAAI ADPNTGFLVG QTQTFPDGSQ QYSEYRIGGT SLAAPVIAAV QALAQEAGGG
KAIGFANPTI YAKYGKKGVF HDVTDNPTGS GLAVARVDFA NGLDAKGGLL YSVRSLGKDS
SLSATKGYDD VTGVGSPADG YVQSYAAKKH
//
