ID   E3T6M6_9BACT            Unreviewed;       419 AA.
AC   E3T6M6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative protease {ECO:0000313|EMBL:ADC35969.1};
OS   uncultured bacterium 98.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=698395 {ECO:0000313|EMBL:ADC35969.1};
RN   [1] {ECO:0000313|EMBL:ADC35969.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kielak A., van Veen J.A., Kowalchuk G.A.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC35969.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20729323; DOI=10.1128/AEM.00343-10;
RA   Kielak A.M., van Veen J.A., Kowalchuk G.A.;
RT   "Comparative analysis of acidobacterial genomic fragments from terrestrial
RT   and aquatic metagenomic libraries, with emphasis on acidobacteria
RT   subdivision 6.";
RL   Appl. Environ. Microbiol. 76:6769-6777(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; GU260706; ADC35969.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3T6M6; -.
DR   MEROPS; M16.A15; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ADC35969.1};
KW   Protease {ECO:0000313|EMBL:ADC35969.1}.
FT   DOMAIN          13..159
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          166..337
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   419 AA;  46416 MW;  40FBEFEEE4A0DB5B CRC64;
     MIVRDVLPNG LRLLTEQMPH VRSVSIGVWL TRGSRHEPSQ HAGIAHFVEH MLFKGTGSRS
     AEDIAQAIDS IGGQMDAFTA KEYASYYIKV LDEHLPLAID VLADIVLRPA FAAEDIEREK
     KVVLEEIKMV EDTPDDLVHE LFTEHFWKDH PLGRPILGTP DTVSALNAET LRSYFTDAYS
     AGNLIVAAVG NIDHSHVRDL VTKHFGHLTT IGEAIVDAPP HVVPEVVIRN KELEQSHVCL
     GTTGYQQDHK DRYASYVLNT VLGGSMSSRL FQNVREKRGL AYAVFSGLSA YRDAGNVTVY
     AGCANNAVAE LIDVVVGELR RIKDDPPPEE EIRRAKDHLK GSLMLNLEST SSRMSHLARQ
     EIYFDRQFGL DETLEGVELV SRADLERVAR DLFGRDALAA TVLGAVNGLE LPRERLSLG
//