ID   DTML_BURM7              Reviewed;         687 AA.
AC   A3MDY1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Dictomallein;
DE            EC=3.4.24.-;
GN   Name=dtmL; OrderedLocusNames=BMA10247_A1281;
OS   Burkholderia mallei (strain NCTC 10247).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10247;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the dictomallein family. {ECO:0000305}.
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DR   EMBL; CP000547; ABO03699.1; -; Genomic_DNA.
DR   RefSeq; WP_004198081.1; NZ_CP007801.1.
DR   AlphaFoldDB; A3MDY1; -.
DR   SMR; A3MDY1; -.
DR   GeneID; 56597480; -.
DR   KEGG; bmn:BMA10247_A1281; -.
DR   OMA; WWTPTVD; -.
DR   Proteomes; UP000002284; Chromosome II.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR019503; Peptidase_M66_dom.
DR   PROSITE; PS51694; PEPTIDASE_M66; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..687
FT                   /note="Dictomallein"
FT                   /id="PRO_0000322653"
FT   DOMAIN          233..501
FT                   /note="Peptidase M66"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   687 AA;  71384 MW;  5FAA5833DB71AC2E CRC64;
     MGNGERPPAR RPDSSGSPPP AADAPAASNH PFSSHDTKHM TSRRLASRTA VAASLSALML
     AACGGDDSAN APTAGGAAPL TPAVASPAGP TGSTPGSTPG ATTAPAPSST SAGQLSVDKM
     AFAQTHVVPS GGLSWTLPNA SASLRPISRR DALVLVAIGQ ADAVQPVLEA WKDGAKLGAL
     ALSPPSALPP TESGGRAYAN DRWSAVVPAA WMVPGVSFSV SASNYTSSVA QAPVFGTDAD
     VQLTILPFYL FGADDTNSPP LSTTQAPDAA TQQEIFAKWP TAELKVRTHP AGRFSLATVV
     VGPRADRTGA AQPAYPVTAL DQQKDGYGVM SAMLTLITNM RTANGDGPLN DQYYAPLIAL
     NSNGQFANLG GGLGGVGSGA AVGDHRYTGI FIHEQGHAFG LNHAGDEYAK GAYPYAGGSL
     SGSVWGYDPN HREFLDVLVP TTASSYAKCA SSHQLDAQGR CYKQDPMQGG AGDQSSGYKF
     ATFSDYNTGR MQAWIASRVL ADPASSTGYS KWDSAAQARA PYTPTTDNNG LYGVNQNLPV
     QAGVPVHTIV VSFSKAGSAG ASYIYPPFSY TGNLIATFDP TSAADRQAIT VDKGTYPWYC
     KGTGCDYTLR VTYADGSRTY RVLQGGFRAW WTPTVYDANA TNPLSGSSFR VWAINVPGDK
     RIGKIELLDT PMVWNGMPAN PTVLLSR