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Database: UniProt
Entry: E0XSX0_9BACT
LinkDB: E0XSX0_9BACT
Original site: E0XSX0_9BACT 
ID   E0XSX0_9BACT            Unreviewed;       542 AA.
AC   E0XSX0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Subtilisin-like serine proteases {ECO:0000313|EMBL:ADI17511.1};
OS   uncultured bacterium HF0130_06E03.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=710813 {ECO:0000313|EMBL:ADI17511.1};
RN   [1] {ECO:0000313|EMBL:ADI17511.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA   Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT   "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT   a 'genome proxy' microarray.";
RL   Environ. Microbiol. 13:116-134(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; GU474867; ADI17511.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0XSX0; -.
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; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR   Pfam; PF13585; CHU_C; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          139..430
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        198
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        382
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   542 AA;  58522 MW;  59E4B4079F747D40 CRC64;
     MGSAHAELVW LLLQDKISPK GRVISWDLSR HTYDVREQDF PVRKDYIREI EEIGVRVRIT
     SRWINAVSVD ASEYQKIQLS KLKFIKSIIP VRRLPKPDKR NGQPLPAGRT AYGNDYYGNS
     YEQLAQVNVI PLHQMGFRGA GIRIAILDNG FHYREHPAFL NGLRVVAERD FINSDAIVSD
     EVGQPYTGDE DRSSQNIHGA QVLSIMAGND IGSFVGVAPD AEYILAKTED NGSEYPIEED
     RWVAGLEWAD SLGADVVNSS LGYNLWDDGS GYNYDDLDGT TALTSVAATL GVKRGLVIVV
     AAGNEGLSSW HYITAPADAD GVTSVGSIAL NTGYESQIRI STTSSRGPTA DGRIKPDLVA
     PGQGVVVADI RSGGYIRNNG TSFAAPIVSG ISALILQINP DLEPNQVLSM LRGSAIDLGD
     SGADTVYGWG LVNALGASGL HMPVPQSTEL NAPSPNPVTG EINQVFFPAN IAEPTNVSLY
     VFDVGGSLVF RQENYFLSGV YQATNGAPAW RLDNSLANGI YFYKLAAGQK TINGTLAIAR
     EK
//
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