ID A0A1B1BDX6_9ACTN Unreviewed; 648 AA.
AC A0A1B1BDX6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ANP57035.1};
GN ORFNames=AVL59_38260 {ECO:0000313|EMBL:ANP57035.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP57035.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP57035.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP57035.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP016279; ANP57035.1; -; Genomic_DNA.
DR RefSeq; WP_067318239.1; NZ_JAGGLP010000003.1.
DR AlphaFoldDB; A0A1B1BDX6; -.
DR STRING; 68214.AVL59_38260; -.
DR KEGG; sgs:AVL59_38260; -.
DR OrthoDB; 3480681at2; -.
DR Proteomes; UP000092659; 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:ANP57035.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:ANP57035.1}; 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_5008519827"
FT DOMAIN 239..648
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 648 AA; 66573 MW; 48C9CCE8348BD4FE CRC64;
MRSNRAKARA GVSMAATLPM IAGALALGIP AAHAADTPAR DALAGTKPAW ATAKADKGAT
ADNAQVNARV YLAGKDRAGL AAYAKAVSDP SSPLYGKYLN AKKAQARFGA TKAQVAAVKS
WLKSAGLQVT EVTAHYVAVS GDVSAAEKAF GTQLHNFTKG GKTYRAPAKS ASAPAGLKGA
VLTVTGLDTA PHKSTHDDQL PPPDAVFKNS GPFSSYYGSK IATTLPDAYG QKIPYAIKGY
TGKQLRSVYG AGDYTGKHVR VAITDAYASP TIAFDAGNYA LKNGDAAWKT GQLHQVLPNN
YTKTKECGAA GWYGEETLDV EAVHAVAPDA DVTYVGAASC YDADLLDSLS KVVDNHLADI
VSNSWGDIEA NQTPDLAAAY DQVFQLGAVQ GIGFYFSSGD DGDQAAKSGT KQVDTPANSA
WVTAVGGTSL AVGKGDSYQW ETGWGTEKAT LSADGKSWTN FPGAFTSGAG GGTSKNVPQP
YYQKGIVPKA LATANNAAGN RVVPDIAAIA DPNTGFLVGQ TQTFPDGTEQ YSEYRIGGTS
LAAPVIAAVQ ALAQEAGGGK ALGFANPAIY AKYGKKGMFH DVTDNPTGSG LAVARIDFVN
GLDATGGLAT SVRTLGKDSS LSAVKGYDDV TGVGSPADGY VQSYGTKH
//
