ID A0A0S7BV18_9BACT Unreviewed; 943 AA.
AC A0A0S7BV18;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Subtilase family {ECO:0000313|EMBL:GAP42395.1};
DE Flags: Fragment;
GN ORFNames=TBC1_11524 {ECO:0000313|EMBL:GAP42395.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42395.1};
RN [1] {ECO:0000313|EMBL:GAP42395.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP42395.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; DF968182; GAP42395.1; -; Genomic_DNA.
DR RefSeq; WP_062038071.1; NZ_DF968182.1.
DR AlphaFoldDB; A0A0S7BV18; -.
DR STRING; 1678841.TBC1_11524; -.
DR OrthoDB; 1652165at2; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR045474; GEVED.
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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF20009; GEVED; 2.
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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..943
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006633232"
FT DOMAIN 192..448
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 575..648
FT /note="GEVED"
FT /evidence="ECO:0000259|Pfam:PF20009"
FT DOMAIN 746..820
FT /note="GEVED"
FT /evidence="ECO:0000259|Pfam:PF20009"
FT REGION 525..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 943
FT /evidence="ECO:0000313|EMBL:GAP42395.1"
SQ SEQUENCE 943 AA; 101354 MW; E64859F702FDEBB7 CRC64;
MKKIHYLLVF CFLMDYAISN PLMAQSGGHE KSSVSHPGYA CEQQWIEVLF DRQSRVRMRN
GTIIDLETNA LEGVASILGA LPWHEWYRMT DLPEPLLDQW EINGEQRTGE DLYNLNNIFR
LKIPRGTDIW SLAAGLESLP GIYLARPVPK PMPLPAMPPG SYQSQQGYLN AASNNPSGVN
ALYAWTQTGG TGTGVTVCDL EYSWNYNHAD LTQAPGSQIN PNAISDPFND NNHGTAVIGE
LVSDNNGWGT TGICYGATLM TCGTYWTSGI GWDVPGAIAY AIASLSAGDI ILLEQQWEYT
SGTQNFIPIE WWTDYSPNQQ SYNGVYAAIV TAIANGIHVV EAGGNGNVNT QNLQWYGNSG
AIIVGAGGAT TSNNLQRLSF SSYGPRFDMQ GWGENVFTTG YGTYYSSEGP NYYYRSDFSG
TSSASPIVAG ALACAQGYYN ANISTIPPTP SYMRSHLATY GTPQVSGPSG NIGPGPDIQA
AILNFPPPQT YYDWGDAPDV PYPTRSANNG AYHLMDGTTY MGNTVDAEND GQPDANATGD
DLNGSNDDDG VVFTSQLIPG QTASVQVTAS VAGWLNAWID FNGLNVWADQ GEFIFQNIQL
SAGVNNLTFA VPPVAVPGQT FARFRFNTYG GILFYGNGGP GEVEDYQVFI SGSGQDEYDW
GDAPDGPYPT LSSGNGARHL IVPGILMGTS IDPEPDGQPD PMCLGDDNDL IYPPPNDDED
GVVFQGQLIP GQPANINVTV SVQGFLNGWF DFNNNGSWLD PGEQLFTDIL IPAGLNPLVM
LIPPTASTGQ TYARFRFSTV QGLSFTGMAP DGEVEDYAVN IEPQPEEFDW GDAPDGPYPT
LGASNGAYHT IVPGFMLGAS IDAEPDGQPD PQALGDDNDI LYPPPNDDED GVTFTSAIVS
GQAATLNIVA SVNGLLNAWI DFNMNGTWSD PNEQIFTDLM LVP
//