ID C1CV85_DEIDV Unreviewed; 712 AA.
AC C1CV85;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative Serine protease, subtilase family, (Peptidase_S8) {ECO:0000313|EMBL:ACO46102.1};
GN OrderedLocusNames=Deide_11940 {ECO:0000313|EMBL:ACO46102.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46102.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO46102.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP001114; ACO46102.1; -; Genomic_DNA.
DR RefSeq; WP_012693225.1; NC_012526.1.
DR AlphaFoldDB; C1CV85; -.
DR STRING; 546414.Deide_11940; -.
DR PaxDb; 546414-Deide_11940; -.
DR KEGG; ddr:Deide_11940; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_417860_0_0_0; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000002208; Chromosome.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..712
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002908139"
FT DOMAIN 302..621
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 573
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 712 AA; 74084 MW; F48A6F087734AD1E CRC64;
MKKLSGSWPI LLTLPLLLAA CTDNFTTPIV EPPVVQPPAP QPPAPQPPAP QPPSASLPAS
VNLGYGFSAP VQAAHSGSWQ VIDQPAWLSV TPTSGTGEIR LAVAADRSKA TPLAADQAKL
TGAVILELTA PDKTRTRATI TVSADQYRMT GRVADTAKIS GQALVTSPIN RARPAEARGI
LVKYRDRVSS SDLVAQSAAQ SPATRSREVL SRAGVTVQSA RSLNGGLAAL KVTDQAAALR
ALRQNPEVEY AVPNAVLHIQ QTSQALAAPL EPTDQYAPLQ WPFKLMGYPA VWRDMESGTY
NRAVTVAVVD SGVRFDHPDL AGQLWGPAEG ALDVLNEPDN GDGDGVDTDP TDPSVSGRST
GSHGTHVTGI IVARWGENAG NCAGCSGTGV VGASYRAPVK VLPIRAIDAT GDATVEHIVQ
ALNYAAGLPT LIGGVTYTNP RRAQVINLSL GGAISAEQAR PLCDAVHAAK SAGSLVFVAA
GNAYGTTPYY PAACPGAVAV GSVTLSGGSA PRHASYSNAY PEVQLSAPGG TDQFSDVFNG
GLLNNKAFPD MVFSTGWDYV KNEPQYEAMS GTSQATPQVS ALAALLLSKG VTSDAAGTLA
RLTATATDLG AQGRDDQFGF GMVNAAAALG APAISDTLGL RLQNARGFVF QPRLDNLGRF
EAYLGDGTFR VVGGRDRDRN QIYGETHEPR DERTVKLGPD TPQVELGTLE PK
//
