ID A0A495W5L9_9PSEU Unreviewed; 601 AA.
AC A0A495W5L9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Subtilisin family serine protease {ECO:0000313|EMBL:RKT55953.1};
GN ORFNames=C8E97_4641 {ECO:0000313|EMBL:RKT55953.1};
OS Saccharothrix australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=2072 {ECO:0000313|EMBL:RKT55953.1, ECO:0000313|Proteomes:UP000282084};
RN [1] {ECO:0000313|EMBL:RKT55953.1, ECO:0000313|Proteomes:UP000282084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43800 {ECO:0000313|EMBL:RKT55953.1,
RC ECO:0000313|Proteomes:UP000282084};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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}.
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:RKT55953.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RBXO01000001; RKT55953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495W5L9; -.
DR OrthoDB; 9766923at2; -.
DR Proteomes; UP000282084; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002884; P_dom.
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; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 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:UP000282084};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..601
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038918153"
FT DOMAIN 482..601
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 601 AA; 61227 MW; CC8C1AB7D30FE0EF CRC64;
MGHVRFIRRT AVLGLAAVSA AGLAFTNVGV AAAEGQVLSA DSADAVPGSY IVALRDSASP
RALSASAADS LVGKYGGAVR TTWQHALNGF HASLSPTQAR RMAADPRVDF VQADLRVQVE
GVQPNPPSWG LDRIDQPNLP LDNSYTYPNG ASDVRAYVID TGIRTTHSDF GGRASWGTNT
VDSNNTDCHG HGTHVAGTVG GTRHGVAKEV KLVAVKVLNC QGQGTSAGVV NGVNWVARNA
VKPAVANMSL GGSADTATDT AVRNLVAAGV TTAVASGNDN QNACNYSPAR VREAISTNAS
TRSDGRASFS NYGTCTDLFA PGQDITSAWH TSDSATNTIS GTSMASPHVA GAAAMYVSAN
PTATPAQVES ALVAAATSGK ITNPGAGSAN KLLFVGGATP DNPVVKNPGD QAGTAGTPVN
LQVTATGGTA PYTFSFTGLP TGVNGSSAGQ VTGTPTAAGT YTVTVTVTDA NSRTGTATFK
WTIRERGDGC DPVTNDTDVA IGDNSDVNST IELTCQGTAS ATAQVTVNIV HSYIGDLVVD
LVAPDGSVYN LHNRAGGSAD NLNRTFTVNT SSETAAGTWK LRVRDLATVD TGRIDSWTLD
A
//
