ID Q9RWC4_DEIRA Unreviewed; 366 AA.
AC Q9RWC4;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=Periplasmic serine protease, HtrA/DegQ/DegS family {ECO:0000313|EMBL:AAF10323.1};
GN OrderedLocusNames=DR_0745 {ECO:0000313|EMBL:AAF10323.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF10323.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF10323.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; AE000513; AAF10323.1; -; Genomic_DNA.
DR PIR; B75481; B75481.
DR RefSeq; NP_294468.1; NC_001263.1.
DR RefSeq; WP_010887390.1; NZ_JMLF01000005.1.
DR AlphaFoldDB; Q9RWC4; -.
DR STRING; 243230.DR_0745; -.
DR PaxDb; 243230-DR_0745; -.
DR EnsemblBacteria; AAF10323; AAF10323; DR_0745.
DR GeneID; 69516990; -.
DR KEGG; dra:DR_0745; -.
DR PATRIC; fig|243230.17.peg.924; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_2_0_0; -.
DR InParanoid; Q9RWC4; -.
DR OrthoDB; 73775at2; -.
DR Proteomes; UP000002524; Chromosome I.
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; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR PANTHER; PTHR43019:SF62; SERINE ENDOPROTEASE DEGS; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:AAF10323.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Protease {ECO:0000313|EMBL:AAF10323.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT DOMAIN 251..339
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 366 AA; 38225 MW; 94A3394D88A06292 CRC64;
MRRFPVLFPL LLLLALTAYL LPARTPQNVE APPPAATTTL PQALPTAERE LFASLRPAVV
RVDSVNTATR TGGLGTGFFI SGEGQVLTAY HVVKAGQLFA VTTLAGKTYP ARVAAFDEAA
DVALLQVARG GPFPYLELAS GTPQVGERVL AIGNSGGDFL QPRRGELLRL NAEAGRSDFP
EGTLEMNAPL AQGDSGGPIF NERGEVLGVV SYIRVSGDGV TRASYAVPVP GGGDLIRGLQ
AGERRESPLT ALVGLAFDQM HSGLTDPPGA VVLRVTPGSA AARAGLRGCV ADRQGQLTGL
GDVILSIGGV RTPDSGTALD QVKRLKVGDQ VDVEYLRGEQ RAHATLTLRA QPVGKTPLNA
EPCTRQ
//