ID B1W2C4_STRGG Unreviewed; 528 AA.
AC B1W2C4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Putative secreted subtilisin-like serine protease {ECO:0000313|EMBL:BAG19288.1};
GN OrderedLocusNames=SGR_2459 {ECO:0000313|EMBL:BAG19288.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG19288.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG19288.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG19288.1; -; Genomic_DNA.
DR RefSeq; WP_003966573.1; NC_010572.1.
DR AlphaFoldDB; B1W2C4; -.
DR MEROPS; S08.051; -.
DR GeneID; 6212096; -.
DR KEGG; sgr:SGR_2459; -.
DR PATRIC; fig|455632.4.peg.2503; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_011263_1_7_11; -.
DR Proteomes; UP000001685; Chromosome.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002772337"
FT DOMAIN 410..528
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 528 AA; 53250 MW; A5F9D478A5AF2568 CRC64;
MSVTRHTPQA RRRLAAATVI ATAAAVALAT AALPATAAER APEGVILNAG APGTISDSYI
VTLKDSAAKS DSAQGKALAK KYGASIERTY RSALNGYAVE ATAAEAKKFA ADPAVASVSQ
NRTFTVSATQ TNPPSWGLDR IDQRSLPLDQ RYTYPDKAGE GVTAYVIDTG VRISHSDFGG
RAANGYDAID NDNVAQDGHG HGTHVAGTVA GTAHGVAKKA KIVGVRVLNN QGSGTTAQVV
AGIDWVTANA VKPAVANMSL GGGADAVLDA AVQRSIAAGI TYAVAAGNES TNANTKSPAR
VAEAITVGST TNTDARSSFS NFGAVVDIFA PGSSITSTWN TSDSATNTIS GTSMASPHVA
GAAAIYLADN PASTPAQVSA GLVAASTPGV VTNPGTGSPN RLLYVGPGGT TPPPGKKFEN
TTGYAINDNA TVEAPVTVTG VTGNAPAALS VPVNISHTYI GDLKIDLVAP DGSVYNLKAY
GSGGSSDNVV TTYTVNASSE VANGTWKLRV SDNASADTGR INSWALQF
//
