ID   K2DEK6_9BACT            Unreviewed;       420 AA.
AC   K2DEK6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   03-MAY-2023, entry version 40.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKD92053.1};
DE   Flags: Fragment;
GN   ORFNames=ACD_29C00217G0001 {ECO:0000313|EMBL:EKD92053.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD92053.1};
RN   [1] {ECO:0000313|EMBL:EKD92053.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD92053.1}.
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DR   EMBL; AMFJ01011630; EKD92053.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2DEK6; -.
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   Gene3D; 1.10.1370.40; -; 2.
DR   InterPro; IPR045666; OpdA_N.
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   Pfam; PF19310; TOP_N; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          37..141
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          214..418
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   NON_TER         420
FT                   /evidence="ECO:0000313|EMBL:EKD92053.1"
SQ   SEQUENCE   420 AA;  48181 MW;  DA935DE718E56E70 CRC64;
     MISDQSLPQF SKINLDMIES NLDKVLEYNL IEINNLLKNN AVYTWDNLMR PMENANDALN
     QFWSPIQHMN AVINSPALRE VVNHCLPKLS DYGTAISQNE GLFHAIESID LKNLDISQRK
     TIENDLRNFK LSGVHLPKDK KNEFATLSKA LSQLTQKFEE NVLDATMGWK KEIMDQAELA
     GIPEHAILNA KLLAEKESKS GWIFNLEAPS YLAVMMYADS QQLRAEMYTA YVTRASNQGP
     NAGKWNNDQV MQDILEKRFA LAKLLGFQNY AEYSLQTKMV KKTNEVLDFL NELAEKSLKP
     AQKEFQALSH FAQSELQLKT LNAWDVAYAS EKFSQKLYQI SPEDLRPYFP EPRVLSGLFD
     VIQKLYGVTI KAADHVDVWH QDAKCFNVFD AHHQLQARLF FDLYARENKR GGAWMDDCKV
//