ID A0A176KXA0_9ACTN Unreviewed; 645 AA.
AC A0A176KXA0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:OAA96922.1};
GN ORFNames=A6P39_30930 {ECO:0000313|EMBL:OAA96922.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA96922.1};
RN [1] {ECO:0000313|EMBL:OAA96922.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA96922.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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:OAA96922.1}.
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DR EMBL; LWRP01000165; OAA96922.1; -; Genomic_DNA.
DR RefSeq; WP_067052968.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176KXA0; -.
DR STRING; 710705.A6P39_30930; -.
DR OrthoDB; 3480681at2; -.
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:OAA96922.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:OAA96922.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..645
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008047503"
FT DOMAIN 238..645
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 645 AA; 66688 MW; EFCDC09A049CE460 CRC64;
MRSNRAKLRA MSMAATLPMV AGALALGIPA AHAADSPARQ ALKGTKPAWA TAKADKGATA
NSAQVNARVY LAGRDAAGLA AYAKAVSDPA SPSYGKYLSA KKAQARFGAT KAQVAAVKSW
LTSAGLTVTS VTQHYVAVSG DAAAAEKAFG TKLHNYAKGS ATYRAPAQAA SVPAALQSAV
LTVTGLDNAP HKANHDDQLP PPDAVFKNSG PFSSYFGSNI ASTLPDAYGQ KIPYAIKGYT
GKQLRAAYGA GSYTGKGVRV AITDAYASPT IAFDAGKYAV TNGDQAWTTG QLHQVLPDKY
SRIKECKAAG WYGEETLDVE AVHAVAPNAD VTYVGSASCY DDDLLDSLAK VVDNHLADIV
SNSWGDTEAS QTPDLAAAYD QVFQLGAVQG IGFYFSSGDN GDEVANTGTK QVDSPANSAW
VTAVGGTSLA VGKDNSYEWE TGWGTEKAVL AADGKSWTNF PGAYTGGAGG GTSKTVPQPY
YQKGIVPKAL ATANNADGNR VVPDIAAIAD PNTGFLVGQT QTFPDGTEQY SEYRIGGTSL
AAPTIAAIQA LAEEARGKAI GFANPLIYAD YGKKGVFHDV TDHPTGTDLA VARVDFANGY
DKAGGLLYSV RSLGKDSSLS AVKGYDDVTG VGSPADGYVQ SYRKH
//
