ID   SUB2_DEIRA              Reviewed;         728 AA.
AC   Q9RYM8;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable subtilase-type serine protease DR_A0283;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=DR_A0283;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
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.A., Utterback T.R., 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.L., 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).
RN   [2]
RP   PROTEIN SEQUENCE OF 149-162.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA   Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT   "Protein recycling is a major component of post-irradiation recovery in
RT   Deinococcus radiodurans strain R1.";
RL   Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AE001825; AAF12479.1; -; Genomic_DNA.
DR   PIR; A75582; A75582.
DR   RefSeq; NP_285606.1; NC_001264.1.
DR   RefSeq; WP_010889542.1; NZ_CP015082.1.
DR   AlphaFoldDB; Q9RYM8; -.
DR   SMR; Q9RYM8; -.
DR   STRING; 243230.DR_A0283; -.
DR   EnsemblBacteria; AAF12479; AAF12479; DR_A0283.
DR   KEGG; dra:DR_A0283; -.
DR   PATRIC; fig|243230.17.peg.3174; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_380248_0_0_0; -.
DR   InParanoid; Q9RYM8; -.
DR   OMA; YEPNDTP; -.
DR   OrthoDB; 923655at2; -.
DR   Proteomes; UP000002524; Chromosome II.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07485; Peptidases_S8_Fervidolysin_like; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034063; Fervidolysin_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR017306; Peptidase_S8A_fervidolysi-like.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF04151; PPC; 1.
DR   PIRSF; PIRSF037882; Subtilisin_rel_fervidolysin; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..148
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:15249204"
FT                   /id="PRO_0000027168"
FT   CHAIN           149..728
FT                   /note="Probable subtilase-type serine protease DR_A0283"
FT                   /id="PRO_0000027169"
FT   DOMAIN          159..471
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        412
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   728 AA;  76755 MW;  D7D51DB5210CB53C CRC64;
     MPGALPMKKI SLAVLSLTTL LAACGQPQTS PQSPAASAPS VAVPRTHALD IDPAQVVTTK
     NGDMYVRNQL VVNLRGHSAD ALADQLGGRV LDQLPELDVA LIELPQGKDA RSVGVALMRE
     GQVLYAAAQT VQRQIEPVRT AQDQLGAQAV NQVFDTLPQY ALDSNHLHAK AAWDAGFTGK
     GVKVGVIDDP SDVSHPDLRP NWAGKAYDPA TNTTYTTVQG WIDAIDGFDG KVDNKVDPGI
     EHGTAVASTI AAAKNGQGIV GVAPDSKFYT AAIFQPGFIG DYLVARSVIW TVNQGAQVIN
     NSWGGTGYSP LLKQAFDYAL ERDITVVVSA GNSYREEWRN PAQLPGVIAS AALDINNDKA
     GFSTYGRHVS VAAPGVDVML ASPLFINADG TRKTGGYTKD GGSGYQLISG TSFSGPYTSG
     VAAVILGAKP DLDPHQVRRL MEETADGSVG SNKAGFDRET GYGLIRMDKL ADRLKGSNMP
     QKGGAGRVKV EIQTPGGYVP GILADVILEG DGADGAVYAV QTDSDGYANF VSIAPGTYTL
     RVATPDLTLT GGQSDERDTY VGKLTVTSGS VLSTVAPQRV VLVKGAVDLN PVDPYEPNDT
     MAEAKPISYG KMTELAYIFG KPRDVDFFSF TGKAGDNIQA DVHARTAIGG SLDSFLVLRD
     ASGKNLAYND DANGQDSVIT FKLPADGTYF LEVSSCNILC KSNGDDASKG QDDDSPFNKY
     VLELQLLK