ID G8SAL8_ACTS5 Unreviewed; 574 AA.
AC G8SAL8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidase S8/S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:AEV87684.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:AEV87684.1};
GN Name=aprA {ECO:0000313|EMBL:AEV87684.1};
GN OrderedLocusNames=ACPL_6802 {ECO:0000313|EMBL:AEV87684.1};
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:AEV87684.1, 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; AEV87684.1; -; Genomic_DNA.
DR AlphaFoldDB; G8SAL8; -.
DR STRING; 134676.ACPL_6802; -.
DR MEROPS; S08.051; -.
DR KEGG; ase:ACPL_6802; -.
DR PATRIC; fig|134676.3.peg.6703; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_1_7_11; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
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; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05345; He_PIG; 2.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
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..47
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 48..574
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003515766"
FT DOMAIN 82..124
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 161..384
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 574 AA; 59029 MW; A26F02A797E8ADEE CRC64;
MVQGVCGLKR GRWRPITRGM RKWTLGALLT SAVAASAALL GPAPALAAGT VIGAELPGAL
PGRYIVTLKD RGTGPSVHSM GAGRLVRSFR SIPGFAAEMT AAQARRLAAD PAVRSVEQDR
MIHIATQNRP GWGLDRIDQR SATLSKTYTA TDDGSAVHAY VIDTGIRITH SEFGGRASYG
YDFADGDRVA SDCNGHGTHV AGTIGGARYG VAKKVQLVAV RVLGCDGGGS ISDVIDGVDW
VTEHAIKPAV ANMSMGGSVS RSLDYAVQES IASGVTYVVA AGNEDDDARW SSPADVPAAI
TVGATDSRDR RASFSNYGSG VDLFAPGVDI RSSVADSNTA TDVYSGTSMA APHVAGAAAL
LLDANPSLTP GQVRDRLVAN ATTGRVADRM GSPNRLLFVT APPAKPVIAT TRTAAAVVGT
ELSTRLALTA NRVGSWTLAG GTLPPGLSLN RSGVLSGTPA QAGDYVVTVR FTDYVPQVVT
RQVTIPVEAS VPVIDPTLPD GQAGVYYEGQ LTTADQRDGV WAVTAGALPA GLTLDEASGL
ISGVPSATGS FTVRFTDPWG QTATADFTIT VGAA
//
