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Database: UniProt
Entry: A9WQW1_RENSM
LinkDB: A9WQW1_RENSM
Original site: A9WQW1_RENSM 
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
//
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