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Database: UniProt
Entry: A0A1Q9LFT0_9PSEU
LinkDB: A0A1Q9LFT0_9PSEU
Original site: A0A1Q9LFT0_9PSEU 
ID   A0A1Q9LFT0_9PSEU        Unreviewed;       579 AA.
AC   A0A1Q9LFT0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:OLR90883.1};
GN   ORFNames=BJP25_30465 {ECO:0000313|EMBL:OLR90883.1};
OS   Actinokineospora bangkokensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR90883.1, ECO:0000313|Proteomes:UP000186040};
RN   [1] {ECO:0000313|EMBL:OLR90883.1, ECO:0000313|Proteomes:UP000186040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44EHW {ECO:0000313|EMBL:OLR90883.1,
RC   ECO:0000313|Proteomes:UP000186040};
RA   Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT   "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT   the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT   extender unit butylmalonyl-CoA.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, 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:OLR90883.1}.
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DR   EMBL; MKQR01000026; OLR90883.1; -; Genomic_DNA.
DR   RefSeq; WP_075977555.1; NZ_MKQR01000026.1.
DR   AlphaFoldDB; A0A1Q9LFT0; -.
DR   STRING; 1193682.BJP25_30465; -.
DR   Proteomes; UP000186040; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; 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   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 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; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000186040};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..579
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039594854"
FT   DOMAIN          462..579
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        394
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   579 AA;  59184 MW;  F37B463FEFB82EDC CRC64;
     MPLRSHPRLR RAATALAVGV GLLTTTAVPA VATPAAASAA AAGLRSYLVI TAPGSTAAAE
     SAVTANGGAV YATYGAIGVV VAHSSAADFA ARVRAVSGIQ QVGATRTVDV PADAANPPIP
     ASPTQVTPTA TETTRADMAQ IGADQAWSVN TGSPSITVGV LDTGVDDQHY DLKANFDAAR
     SASCAYGKLD TRPGAWRPVG EHGTHVAGTI AAARNGKGMV GVAPTVKIAS VRVAERDTQL
     FYPENTICAF VFSADQGMKV TNNSYYTDPW LFNCPTDLDQ AAILEGVKRA TAYAEGKGVL
     NVAAAGNENY NLANKTTDTT SPDDSTPVTR TITTSCLAVP NELPAVLPVS SITSSNTKSS
     FSNYGTDKVV VAAPGDAVYS TLPGGRYGSL SGTSMASPHV AGVAALLASV DPAATPAQLR
     ARLQSQADDL PCTDTRCTGT TAKNNFFGEG RVDAKEAVST PTTPGPSFTN PTDVPIPDAG
     AAVTSPITTT GLTGNAPATL KVAVTIVHTY RGDLVLDLLA PDGTAFPLKS ANSGDSTPNL
     STTYTVNAST KPATGTWKLR ARDAFRSDTG YIDSWTLTF
//
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