ID A9WQW1_RENSM Unreviewed; 240 AA.
AC A9WQW1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Serine protease, trypsin family {ECO:0000313|EMBL:ABY23634.1};
DE EC=3.4.21.4 {ECO:0000313|EMBL:ABY23634.1};
GN OrderedLocusNames=RSal33209_1901 {ECO:0000313|EMBL:ABY23634.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23634.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP000910; ABY23634.1; -; Genomic_DNA.
DR RefSeq; WP_012245305.1; NC_010168.1.
DR AlphaFoldDB; A9WQW1; -.
DR STRING; 288705.RSal33209_1901; -.
DR MEROPS; S01.103; -.
DR KEGG; rsa:RSal33209_1901; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_006842_7_0_11; -.
DR OMA; SALPWIN; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 2.
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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ABY23634.1};
KW Protease {ECO:0000313|EMBL:ABY23634.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..240
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002744126"
FT DOMAIN 37..240
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 240 AA; 24300 MW; D117DE5FEFB62A72 CRC64;
MRKSVKAALF RMVAFGLVFT GTSAATASVS TPPSPRIVGG TTASINDFPS IVAVNQSNGS
NWCGGTLIAI NAVLTAAHCV DGKSASFFKV NGGSANRTGG PNSSTVKSVW MNPSYDGSTY
ENDFAVPTLN TSFSGPVATL ETDPSVYAAG TNATVLGWGD TSSGAGNYQS KLRKVTVPIV
SDSACASSYP QGSSKGTYFE DSMVCAGLPQ GGKDSCQADS GGPLVIGGKL VDAIKGQIAK
//