ID H8H2M7_DEIGI Unreviewed; 346 AA.
AC H8H2M7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN OrderedLocusNames=DGo_PB0505 {ECO:0000313|EMBL:AFD27774.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG Plasmid P2 {ECO:0000313|EMBL:AFD27774.1,
OG ECO:0000313|Proteomes:UP000007575}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD27774.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD27774.1, 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 P2 {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 S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR EMBL; CP002193; AFD27774.1; -; Genomic_DNA.
DR AlphaFoldDB; H8H2M7; -.
DR KEGG; dgo:DGo_PB0505; -.
DR PATRIC; fig|745776.4.peg.3788; -.
DR HOGENOM; CLU_801057_0_0_0; -.
DR OrthoDB; 9766361at2; -.
DR Proteomes; UP000007575; Plasmid P2.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR008256; Peptidase_S1B.
DR PANTHER; PTHR43019:SF23; PROTEASE DO-LIKE 5, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Plasmid {ECO:0000313|EMBL:AFD27774.1};
KW Protease {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:AFD27774.1};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
SQ SEQUENCE 346 AA; 38443 MW; 4EDF48B4CD64D153 CRC64;
MKKSSSIYTS DDRIADTLLE YFRIENSIVD PSKVSERDQS RIKRLDVEGQ RKSLIFKNVL
DFIRDKAVSP IADTLKYEYF CKKLVSEGLL VQMGQSNLNL FSVGEYLTES YEESIAEYGG
YTLLINGFKS VRDYCIRSVT PIETYTELED NGEHKGIGTA FYIGDNMFVT AKHVLKDTQK
FRLLLDGEML NVTNITFSDD LKLDIALISV ESPKVLSLPA IRLGTGMVLD DIIAMGFPKI
TSGISEVVVT TSGEIVAEDY IYSAGRRMHI INAKVKGGNS GGPILNSLGQ AVGIVTNDEL
DEYNQGNVFG LAVPSEEITK ILNSTDKIVK PVRSHNGWSS FRKDNI
//
