ID G8S8Y9_ACTS5 Unreviewed; 674 AA.
AC G8S8Y9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Protease {ECO:0000313|EMBL:AEV87586.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:AEV87586.1};
GN OrderedLocusNames=ACPL_6704 {ECO:0000313|EMBL:AEV87586.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV87586.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP003170; AEV87586.1; -; Genomic_DNA.
DR RefSeq; WP_014693650.1; NZ_LT827010.1.
DR AlphaFoldDB; G8S8Y9; -.
DR STRING; 134676.ACPL_6704; -.
DR KEGG; ase:ACPL_6704; -.
DR PATRIC; fig|134676.3.peg.6599; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_441907_0_0_11; -.
DR OrthoDB; 5240330at2; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 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; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034084; Thermitase-like_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..674
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003516696"
FT DOMAIN 139..389
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 405..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 341
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 674 AA; 66700 MW; FF6A0037609A825C CRC64;
MKVVLRRYAV GAVAAAAVAG VAAFALPTGT VGWTPVTYGL HQTADQLLPA TVTAEQPARV
VGTTIDRNGK PVVTVREATT RDGAAKLVEQ AQKAENAVGV EIDAKAVALD AVTGGDLYRP
QQWDLARMRA TDAWPTSTGA GVTVAVIDTG VDASNVDLTG KVLTGWDAVA DKPGGNTDQN
GHGTHVAGTI GAVTGNTVGV SSVAPDTRIL PVKVLGADGS GYMSDTAEGI IWAADNGAQV
INMSLGSTSQ VGAVSNAIAY ARSKGVTVVA AAGNERANGS PVSYPGADAG VIAVAATDSA
DNVASYSNAG GYVDVAAPGS AILSTYPSAL GRSYATMSGT SMASPHVAGL VALLKSVNGG
LTPDQLEQAL ETSAVDLGTP GRDDDYGYGR VDAVAALAAV TAAPSSAPTS APTSAPTSAP
TSAPTSAPTS APTSAPTSAP TSAPTSAPTS VPTSAPVSKA PTAAPTTAPT SKAPTASPTT
APTSKAPTAA PSPTVAKAKP VIVANPARAD VNYGTTNVTT FTVTAAGQPW VKKNAQLCVA
ESGKAFQCVD VVTSATGTVT ANRVATAGYQ LELRIAATTA NEAATGAAAY TVHSSAYAVR
TGTRTMSVSL ASPAGLNVEV QQLIGGSWKK VLQFASNATT TKATVSGLTT GQQYRVVVPT
TGSITGSTSS IVVA
//
