ID A0A0D7CSG8_9ACTN Unreviewed; 651 AA.
AC A0A0D7CSG8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KIZ18347.1};
GN ORFNames=SNA_06880 {ECO:0000313|EMBL:KIZ18347.1};
OS Streptomyces natalensis ATCC 27448.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1240678 {ECO:0000313|EMBL:KIZ18347.1, ECO:0000313|Proteomes:UP000032458};
RN [1] {ECO:0000313|EMBL:KIZ18347.1, ECO:0000313|Proteomes:UP000032458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27448 {ECO:0000313|EMBL:KIZ18347.1,
RC ECO:0000313|Proteomes:UP000032458};
RA Mendes M.V., Beites T., Pires S., Santos C.L., Moradas-Ferreira P.;
RT "Draft genome sequence of Streptomyces natalensis ATCC 27448, producer of
RT the antifungal pimaricin.";
RL Submitted (SEP-2014) 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:KIZ18347.1}.
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DR EMBL; JRKI01000009; KIZ18347.1; -; Genomic_DNA.
DR RefSeq; WP_044363814.1; NZ_JRKI01000009.1.
DR AlphaFoldDB; A0A0D7CSG8; -.
DR PATRIC; fig|1240678.4.peg.1441; -.
DR Proteomes; UP000032458; 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:KIZ18347.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KIZ18347.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..651
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038696707"
FT DOMAIN 243..651
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 651 AA; 67885 MW; 047F61C71C6F8E9B CRC64;
MRSSRTRTPR VRTGLAWAAA LPLVAGTLAF GAPAADAADH DGGRHALLGT KPLWATSKAD
QGATSGSTDI TARVYLAGRD AKGLAGYARA VSDPHSSSYG KYLSAAQVRA RYGATHDQIS
KVTDWLKNSG LKVTGTTNRY VTVTGDAAAT ERAFATDLHN YRKSGHTYHA PSVTASAPAS
LADAVLTVTG LDNAPRFSQH HTQLPPPSPV FRNSGPFSSY YGSRTDASLP SAYGSKAPYA
IKGYTGKQLR AAYGAKKWTG KRVTVAITDA YASPTIAPDA AKYAARQGDQ AYRGGQLSQV
LPKAYTHIKD CGAAGWYGEE TLDVEAVHAV APDSDIVYVG AASCQDDDLL DSLGKIVDGH
LADIVSNSWG DIEASETPDS AAAYDQLFQQ GAVQGIGFYF SSGDNGDEVA NTGIKQVDTP
ANSAWVTAVG GTSLAVGKRD AYKWETGWGT QKAVLSKDGK EWTDFPGAFN GGAGGGVSKT
VPQPYYQRGI VPDQLSSVLL KGKMRAVPDI AAVADPNTGF LVGQTQTLPD GKLGYDEYRI
GGTSLAAPVI AGVQALAQQA RHGVPLGFAN PAIYQRYGTS AYHDVTDHPL GAGRGLAVVR
VDYVNGADAS KGTTTSLRSL GKDSSLKAVV GYDDVTGVGS PGAGYVSSYR P
//
