ID A0A0S7BWJ4_9BACT Unreviewed; 693 AA.
AC A0A0S7BWJ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Zn-dependent oligopeptidase {ECO:0000313|EMBL:GAP42546.1};
GN ORFNames=TBC1_11677 {ECO:0000313|EMBL:GAP42546.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42546.1};
RN [1] {ECO:0000313|EMBL:GAP42546.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP42546.1};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; DF968182; GAP42546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7BWJ4; -.
DR STRING; 1678841.TBC1_11677; -.
DR PATRIC; fig|1678841.3.peg.766; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 241..689
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 693 AA; 78324 MW; 235BA0CDCF01725E CRC64;
MITACKTGGN EKSAVENPFL TEYNTPFGVP PFGEIKNEHF LPAIEKGIVE QTAEIAAIVS
NPEPADFENT IAAFDYSGEL IRKVTGVFYN YNSSNTNDEI QALAKEIAPK LSAHYDNINL
NPDLFERVRT VYENRNSLNL SGEQARLLED TYKDFVRGGA ALDSSAQARF REINQELSVL
TLRFGENVLA ETNAFKLVIE NQDDLEGLTQ GLIDQGAETA KAAGMEGKWV YTLHNPSIMP
FLQYSAKREL REKIYKAYIN RGNNNNDKDN KELIGKIAAL RLERANLLGY ESHAAFILEE
NMAKNAGNVL DLLNKLWTPA LKRAKGEVAQ LQAIIDKEGG SFKLQPWDWS YYAEKLRKEQ
YDLDDEQLKP YFSLENVKQG IFTVCNNLYG ITFNEQKDIP VYHPEAVAYE VKEANGDHIG
VLYMDFHPRE SKRGGAWMSS YRKQYVKNGE KISPVITIVC NFTKPTASQP SLLTFDETST
FFHEFGHALH GLLSNSTYFS LSGTSVPRDF VELPSQIMEN WASEPEVLKL YAKHYQTGEV
IPDELIEKIQ NSAYFNQGFA TVEYLAASFL DMGYHNMKEF SLTDVSSFED ATLAQIGLIP
EITSRYRSTY FNHIFSGGYS SGYYSYIWSG ILDSDAFEAF KEHGLFDHAT AESFRKNILE
RGGTEDPMVL YKKFRGAEPD IKPLLKRRGL LES
//
