ID K0K511_SACES Unreviewed; 517 AA.
AC K0K511;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Secreted serine protease {ECO:0000313|EMBL:CCH33401.1};
GN OrderedLocusNames=BN6_61490 {ECO:0000313|EMBL:CCH33401.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH33401.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH33401.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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; HE804045; CCH33401.1; -; Genomic_DNA.
DR RefSeq; WP_015103512.1; NC_019673.1.
DR AlphaFoldDB; K0K511; -.
DR STRING; 1179773.BN6_61490; -.
DR KEGG; sesp:BN6_61490; -.
DR PATRIC; fig|1179773.3.peg.6195; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_011263_1_7_11; -.
DR OrthoDB; 9766923at2; -.
DR BioCyc; SESP1179773:BN6_RS29595-MONOMER; -.
DR Proteomes; UP000006281; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 386..517
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
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 517 AA; 52330 MW; 5F5BBB5A04DF887B CRC64;
MRHDRSTPRR VVTACLATSA LMAGVGYGYG YAAEGAIRGA DAPGAVKDAY IVVFKDSAVG
APQAPAKAGD LAAKYGGKVK LTYTAALRGF SVSMSEAQAR KLAADPAVDY VEQDGIAKAT
GVQDNPTWGL DRVDQKNLPL DKKYNYANTA SNVTAYVVDT GVHKAHSDFG GRAVDGYDFI
DNDSVAQDCN GHGTHVAGTI GSTTYGVAKG VKLVGVRVLN CQGQGEWSQV IGGIDWVAKN
AVKPAVANLS LGGGADSSVD NAVKRAVAAG VTFAVAAGND NKDACSTSPA RTPEAITVNA
TDSSDTRSTF SNYGSCTDIF APGTGITSTW NNGSTNSISG TSMATPHVAG AAALYLSGNT
SATPAQVSKA LTDNATSGVV KNAGSGSPNK LLYTGFIGDS GPCSGGSNAD DVAIPDAGSA
VSSSVTVTGC EGVGSASTSV KVDINHSYTG DLAIDLVGPS GNAIVLRKAG GVGSASGIHE
TFTVNTGPEN KNGTWKLRVT DVYSYDTGNV DGWSLSF
//
