ID   B1TCQ6_9BURK            Unreviewed;       151 AA.
AC   B1TCQ6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:EDT38663.1};
GN   ORFNames=BamMEX5DRAFT_5572 {ECO:0000313|EMBL:EDT38663.1};
OS   Burkholderia ambifaria MEX-5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT38663.1, ECO:0000313|Proteomes:UP000004814};
RN   [1] {ECO:0000313|EMBL:EDT38663.1, ECO:0000313|Proteomes:UP000004814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEX-5 {ECO:0000313|EMBL:EDT38663.1,
RC   ECO:0000313|Proteomes:UP000004814};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Tiedje J., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT   5.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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:EDT38663.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABLK01000261; EDT38663.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1TCQ6; -.
DR   PATRIC; fig|396597.7.peg.2039; -.
DR   Proteomes; UP000004814; Unassembled WGS sequence.
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; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
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   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          1..144
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   151 AA;  16468 MW;  FFD72A74F22D891C CRC64;
     MLAARHVDHG IEMAHQIALS ALDLELHSAR AMASNQSILH WVEAIHRAYE ATPPDPLSRS
     VNTFGHIFAG DYAAAYYSYQ WAKVLAADAY AALENAGATH ANAGGREMGK RYRTEILGPG
     GSRPAMESFI AFRGRAPDLD ALFRDSVATR R
//