DTML_BURP6
ID DTML_BURP6 Reviewed; 687 AA.
AC A3NKA8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Dictomallein;
DE EC=3.4.24.-;
GN Name=dtmL; OrderedLocusNames=BURPS668_A1784;
OS Burkholderia pseudomallei (strain 668).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=668;
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; CP000571; ABN85870.2; -; Genomic_DNA.
DR RefSeq; WP_004536510.1; NC_009075.1.
DR AlphaFoldDB; A3NKA8; -.
DR SMR; A3NKA8; -.
DR MEROPS; M67.A13; -.
DR EnsemblBacteria; ABN85870; ABN85870; BURPS668_A1784.
DR GeneID; 56530323; -.
DR KEGG; bpd:BURPS668_A1784; -.
DR HOGENOM; CLU_451780_0_0_4; -.
DR Proteomes; UP000002153; 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_0000322658"
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; 71308 MW; 5C6697275DA807CE 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 VTYADGSQTY RVLQGGFRAW WTPTVDDANA TNPLSGSSFR VWAINVPGDK
RIGKIELLDT PMVWNGMPAN PTVLLSR