ID K0JTF5_SACES Unreviewed; 1055 AA.
AC K0JTF5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Peptidase S8/S53, subtilisin kexin sedolisin {ECO:0000313|EMBL:CCH29186.1};
GN OrderedLocusNames=BN6_18660 {ECO:0000313|EMBL:CCH29186.1};
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:CCH29186.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH29186.1, 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; CCH29186.1; -; Genomic_DNA.
DR AlphaFoldDB; K0JTF5; -.
DR STRING; 1179773.BN6_18660; -.
DR KEGG; sesp:BN6_18660; -.
DR PATRIC; fig|1179773.3.peg.1873; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_007528_0_0_11; -.
DR OrthoDB; 9795680at2; -.
DR BioCyc; SESP1179773:BN6_RS09165-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1055
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038834736"
FT DOMAIN 193..448
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
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 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1055 AA; 107961 MW; 866C8DD4CB591DDB CRC64;
MTPPRGRGAL CAALALFGLV TAATPAGGRS PAGEVAAGAR SITLVTGDRV VLTGDQVGSL
TGGPGRERAV FHTFRRDGHL HVVPRDAAHD LARGRLDPRL FDVTALLEAG YDRRPTIPLI
VVGDPGLPRT KTLDAVGAVA VEVPKGGAAD AWRTLVSRAS VRKVWLDGLR RPSLDRSTAQ
IGAPAAWSAG YTGEGVKVAV LDTGIDDGHP DLAGRVAARS NFTTDPDNTD RVGHGTHVAA
AIGSRHAVYR GVAPDAELLD GKVCVAAGCP ESAILAGVQW AVGQGADVVN LSLGGPDTPE
TDPLEAAVEA LSARALFVVA AGNSGRPGTV SSPGSADAAL TVGAVDRAEG IAEFSSRGPR
PDGGVKPDVT APGVDIAAAK AEHGTIGTPV DATHVALSGT SMATPHVAGA AALLAQQHPD
WSGARLKAAL VASARPNPAL TAFDQGAGRV DLAAAITTTV TADPANVALG LQKWPHDDDT
PVTKNVVYRN TGTAPVTLRP SAVVTAPDGK PSDVVTVSPA EVTVPPGGDA TIAVTADTRR
APVDGVYAGT IVATGGATPL RVPVSVHREV ESYDVTFRFV DAAGNPAKNY YASVIGMDNS
TFVFLFSADG KVSLRVSKGD YFVGADVTTD RKVALLPRPD LSVTADTTVV VDARTARPVR
ITAPDPKARE VLGDLTTARR RGDRSASVST AFLGGFGTDV SIGHNGPDLP GEELTALLGA
QLSGTPAGPT PVTYRFAWAL HGRLPTGFAR AVPAEDLAEV RTSYGAGPAG STYGHVGNPA
APDGTTGWGW MPAVAGASVD RVGTEGVGWS WGFQQTAADG STALSLVAPE RSYRKGSTVQ
ERFNDPVFSP VLPVGRPTSL ARKGDEIGFG LPLFGDGAGN GGSSAVSSAR TTLLRDGVRV
GETAFPGNGL FKVPGGAADY RVETEAARPA GVSEFATRVA AAWTFRSDTA PGGELRPLPL
TVVRFAPELT AGSAPRGAEL RVPLVVRQQA TDGIGRLDVE VSFDDGRTWA AVPVSDGVAR
VANPDAAGFA SLRVRASDRV GNTAEHTVIR AYKIV
//
