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Database: UniProt
Entry: C9Z0K0_STRSW
LinkDB: C9Z0K0_STRSW
Original site: C9Z0K0_STRSW 
ID   C9Z0K0_STRSW            Unreviewed;       271 AA.
AC   C9Z0K0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Putative secreted serine protease {ECO:0000313|EMBL:CBG69553.1};
GN   OrderedLocusNames=SCAB_24411 {ECO:0000313|EMBL:CBG69553.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69553.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG69553.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG69553.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; FN554889; CBG69553.1; -; Genomic_DNA.
DR   RefSeq; WP_013000245.1; NC_013929.1.
DR   AlphaFoldDB; C9Z0K0; -.
DR   STRING; 680198.SCAB_24411; -.
DR   MEROPS; S01.102; -.
DR   GeneID; 24310053; -.
DR   KEGG; scb:SCAB_24411; -.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_006842_7_0_11; -.
DR   OMA; TRAGQFC; -.
DR   Proteomes; UP000001444; 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; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF98; FI18310P1-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; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:CBG69553.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..271
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003004225"
FT   DOMAIN          31..271
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   271 AA;  27260 MW;  DCCE11213F6A6532 CRC64;
     MRRSFARLLA VAATTAVIPL AAPPPASAEV VIGGHPVEIS QAPWTVALAS RDRFGGTRAG
     QFCGGVVIGR STVLTAAHCL SESVLGGPPE RVGDLRVIAG RAELQSAEGQ EIAVSGAWVD
     PAYDPYTNAG DFAVVTLASP LPETSVIGLA EAGDPAYGPG TPAAVYGWGD TTGAGDYGRS
     LRAAPVQVLA DEVCEKAYPG SADGRYLSGS MVCAGEQDGG RDACQGDSGG PLVAQGKLIG
     LVSWGSGCGL AGSPGVYTRG SYIARVLTGS R
//
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