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Database: UniProt
Entry: A0A1W2BY97_9PSEU
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Original site: A0A1W2BY97_9PSEU 
ID   A0A1W2BY97_9PSEU        Unreviewed;       519 AA.
AC   A0A1W2BY97;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SMC77724.1};
GN   ORFNames=SAMN05660733_01635 {ECO:0000313|EMBL:SMC77724.1};
OS   Lentzea albidocapillata.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=40571 {ECO:0000313|EMBL:SMC77724.1, ECO:0000313|Proteomes:UP000192840};
RN   [1] {ECO:0000313|Proteomes:UP000192840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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; FWYC01000005; SMC77724.1; -; Genomic_DNA.
DR   RefSeq; WP_030481558.1; NZ_JOEA01000030.1.
DR   AlphaFoldDB; A0A1W2BY97; -.
DR   STRING; 40571.SAMN05660733_01635; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG4935; Bacteria.
DR   OrthoDB; 9766923at2; -.
DR   Proteomes; UP000192840; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..519
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010705122"
FT   DOMAIN          399..519
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        187
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        342
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   519 AA;  53110 MW;  2D0B6E6214FC5D9A CRC64;
     MRLDRTTRVL AAAGLGLAVA AAVSSPVSAQ TGSIQKSDKP VAGSYIVVFK DGATDVPTTN
     AKALGLARKH GGKVSNTYVA SVRGFAVKLD EAAARRLAAD PSVAYVQQDG WASISDTQTN
     PTWGLDRIDQ ANLPVDQKYT YPNTAPTVTA YILDTGIYKA HSDFEGRATD GYDFIDNDPD
     ASDCQGHGTH VAGTVGSKTY GVAKKVNLVG VRVLDCSGNG QYSQIIKGID WVAQNAKKPA
     VANMSLGGGA DSTVDSAVQR AIATGVTFGL AAGNNNGNAC NTSPARVPEG ITVAASDSAD
     KRSIYTGGQA SNWGSCVDLF GPGSNITSTR NGGGTTSMGG TSMATPHVVG AAALYLSANP
     SATPAQVRDA LVNNATTGKI TDLQGSPNKL LNISFIGGGG PDPECPAATN GDDVSIPDTN
     TAVTSSVSVT GCTGKASATT KVKVDINHPY TADLAIDLVG PSGATYSLKK AKGATSSAGV
     HETFTVDASA ENRDGTWKLQ VTDVWTYDAG NIDTWTLTF
//
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