ID A9WPP6_RENSM Unreviewed; 605 AA.
AC A9WPP6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:ABY23004.1};
GN OrderedLocusNames=RSal33209_1267 {ECO:0000313|EMBL:ABY23004.1};
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:ABY23004.1, 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 S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP000910; ABY23004.1; -; Genomic_DNA.
DR AlphaFoldDB; A9WPP6; -.
DR STRING; 288705.RSal33209_1267; -.
DR KEGG; rsa:RSal33209_1267; -.
DR eggNOG; COG0265; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_020120_3_2_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ABY23004.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ABY23004.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 200..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 495..590
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 60852 MW; 24B25E77036F699B CRC64;
MNQDHNEQSR GQRMSDQING PTPNEENKQP KHGWWDSVEG GNESKSEAAD GAAVSPESSA
AQHSEPSEAS PLETNQTETH QTERLSQSSF TSPSQSWADS QPTEPQPTEP ISAQPADPQP
TQPQPMLPTQ PVHQPRHGQY AGGASYGTQP GHEVPTANQT PGATPHYGQA GACNGAFGTP
TPAPGASPVK TEKKRFGAGV LISGMVIAAL IGGGAAAGSS ALLNGNRSSS VSQQQNQNAP
VVVNNPDKVN AVTVAAQKAS PSVVTIAVSS GNSAGSGSGI ILDTDGNILT NTHVVTLDGK
VANPTLQVKL NDGRLFNAKV VGTDPLNDLA VVKIDAPNLT PAELGDSSKT NVGDTVIAIG
TPLQLSLSNT VTDGIISSNN RTISVASSAA PKSQGDTSSD GSSSKGNGGF NFAPPDGSTP
NSSAQGSINL NVIQTDAAIN PGNSGGALVN SSGQVIGVNV AIAGASSGSS EGSSGNIGVG
FSIPINTAKW VSQQIIKNGS ATHGMLGVSV QPKAPGDDSS SNQQSSSQFS VGALVASVTD
GSAASKAGLK QGDVITNFGS RVIDDASSLT AAVMEQQAGA TVKVTFTRGG QSQSVDVTLD
AKSNG
//
