DTML_BURMA
ID DTML_BURMA Reviewed; 687 AA.
AC Q4V2J8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Dictomallein;
DE EC=3.4.24.-;
GN Name=dtmL; OrderedLocusNames=BMAA1111;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY59193.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000011; AAY59193.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004198081.1; NC_006349.2.
DR RefSeq; YP_338443.1; NC_006349.2.
DR AlphaFoldDB; Q4V2J8; -.
DR SMR; Q4V2J8; -.
DR STRING; 243160.BMAA1111; -.
DR PRIDE; Q4V2J8; -.
DR EnsemblBacteria; AAY59193; AAY59193; BMAA1111.
DR GeneID; 56597480; -.
DR KEGG; bma:BMAA1111; -.
DR PATRIC; fig|243160.12.peg.4649; -.
DR eggNOG; ENOG502Z8SD; Bacteria.
DR HOGENOM; CLU_451780_0_0_4; -.
DR Proteomes; UP000006693; Chromosome 2.
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_0000322651"
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