ID K0K116_SACES Unreviewed; 273 AA.
AC K0K116;
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=Secreted trypsin-like serine protease {ECO:0000313|EMBL:CCH32031.1};
GN OrderedLocusNames=BN6_47560 {ECO:0000313|EMBL:CCH32031.1};
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:CCH32031.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH32031.1, 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 S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE804045; CCH32031.1; -; Genomic_DNA.
DR RefSeq; WP_015102143.1; NC_019673.1.
DR AlphaFoldDB; K0K116; -.
DR STRING; 1179773.BN6_47560; -.
DR KEGG; sesp:BN6_47560; -.
DR PATRIC; fig|1179773.3.peg.4764; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_006842_7_5_11; -.
DR OrthoDB; 3657335at2; -.
DR BioCyc; SESP1179773:BN6_RS23005-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51318; TAT; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCH32031.1};
KW Protease {ECO:0000313|EMBL:CCH32031.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..273
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003834002"
FT DOMAIN 35..270
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 273 AA; 28517 MW; 410445EEB60B2797 CRC64;
MPTVKSMRRT LLRAAAVAVA VGVCTTLTTG GASAVVNGKD STERYQFMAS IPETVPALGG
VKGVCGAALI HPRWVVTAAH CVDAAGTGAV PDGIVRIGSE RRTSGGSVRA IDRTVLHPDY
RLGQPNRGDI ALVRLDRPVL QQPIRIASRP GAPGTPTRLL GFGTTLDTVD ITKAVFPDRL
QQLDTRRGAE SECAPGYADP TRLCTVSRKP GAMACVGDSG GPQVQRGKGG RWELIGTTSG
PGDADAVCAN GPGLYTNVPA HARWIHETIR ANR
//
