ID T1RQV7_9BACT Unreviewed; 770 AA.
AC T1RQV7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:AGN12835.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AGN12835.1};
RN [1] {ECO:0000313|EMBL:AGN12835.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24024096; DOI=10.1186/2193-1801-2-410;
RA Biver S., Portetelle D., Vandenbol M.;
RT "Characterization of a new oxidant-stable serine protease isolated by
RT functional metagenomics.";
RL Springerplus 2:410-410(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KC433657; AGN12835.1; -; Genomic_DNA.
DR AlphaFoldDB; T1RQV7; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR034058; TagA/B/C/D_pept_dom.
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; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 282..642
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 326..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 584
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 770 AA; 82430 MW; AC9D3E0797EFC0D9 CRC64;
MARVLKVFGS AEERKQLAAK HKLLADYDAF TLLEVADQHA KRVARSHLVE DITQQYRLPI
GDTVADTRQP RITARGVARP HRAYEGVKSP GPGRHHYVVQ FVGPIKKAWL TRVRKAGGEP
RVPYEGFAYV VRMDKKALAA VAALPVVRWV GHLPASARVA AGTRRRTEGG RRARAIEATV
PRTQIRPGVY TVQFFGPDDL SKGLSSVRKL GFKILDRPHD PRLLIVESQK PEASREGQLD
RLAAVHGVRE VRERAIKRPS NDVSAGLMGA PVVMGAGFNL SGEGEIICVC DTGLDTGDPA
TIHPDFSGRI EAIRSFPITP DFAPFVNNPG ANDGASDRDS GHGTHVSGSV LGDGTSSAGL
TGLAGPIRGL SHKARLVFQA IEQEIDWKNP ADEQRYGRFL LAGIPTDLAV LLQDAYSRGA
RIHSNSWGGG DPGAYDAMCE QLDRFVWQHK DMCVLFAAGN DGTDQDGDGV INPMSVTSPG
TAKNCITVGA SENDRSEFDA ETYGKWWPTD YPAAPYKNGA MADDGGQIVP FSSRGPTADG
RFKPDVLAPG TFILSTRSTR IALNNKAWAA FPQSRLYFHM GGTSMATPLT AGAVGLLRQY
VGKKRVAGGA TAALLKALLI ASTVRLTVTG PNRVVDNDQG YGLINLASAL KPSKSRKLRM
HNVSPGLSTG QAWSRTIKVS GSAPLRVVLA YSDFPGPALV NNLNLMVTGP DGTRFVGNQP
QAGSVTLDSA NNVELVDVPS AASGHWRIDV VGANVPEGPQ EFALVIVGRT
//
