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
//