ID H8H134_DEIGI Unreviewed; 434 AA.
AC H8H134;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Peptidase S8, subtilisin {ECO:0000313|EMBL:AFD27053.1};
GN OrderedLocusNames=DGo_PA0167 {ECO:0000313|EMBL:AFD27053.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG Plasmid P1 {ECO:0000313|EMBL:AFD27053.1,
OG ECO:0000313|Proteomes:UP000007575}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD27053.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD27053.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RC PLASMID=Plasmid P1 {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP002192; AFD27053.1; -; Genomic_DNA.
DR RefSeq; WP_014695571.1; NC_017805.1.
DR AlphaFoldDB; H8H134; -.
DR KEGG; dgo:DGo_PA0167; -.
DR PATRIC; fig|745776.4.peg.3203; -.
DR HOGENOM; CLU_011263_0_0_0; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000007575; Plasmid P1.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Plasmid {ECO:0000313|EMBL:AFD27053.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..434
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003613155"
FT DOMAIN 166..405
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 175
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 434 AA; 44161 MW; 796D9985569918D8 CRC64;
MTHRLPAAFA LLTLSLLSAC STANVPAQTA QAPVRYESVV SVPLQAGDTR ESLAHAVGGE
VLAWNAGGCA TGDVNDCTAL IGFNPKLGSA SVISALGGRK AKVEANKNVF RGGDKITAVA
NGGAAIWAVG GAAIWAVGQY NPISQNNALW QQVKLEQAQQ MATHLGEGVT VAVIDSGIDL
QHPAFQGALS DASTWHDFYA GDDVPQEEGV AGEGAYGHGT NVAGIILQVA PKAKIMPLRV
LGADGSGDVA SVAQAIRWAV EKGAKVINLS LGSTENSPAV QIAIDWATAQ DVLVVAAAGN
ENKDHITYPA ANATHGVAAP NLLSVGSVDP QDLKSSFSNY SAALEIVGPG EHVYAPAPDG
RMASWSGTSM AAPMTAGGLA LALGETLKVP VRSLTGAMAQ TADDIYGGEA NAAYTGLLGK
GRLNLAAFLG QTIR
//
