ID A2SHV6_METPP Unreviewed; 323 AA.
AC A2SHV6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000256|ARBA:ARBA00017223};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE AltName: Full=B2 metallo-beta-lactamase {ECO:0000256|ARBA:ARBA00030107};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000256|ARBA:ARBA00033087};
GN OrderedLocusNames=Mpe_A2189 {ECO:0000313|EMBL:ABM95145.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95145.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95145.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001526};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Class-B
CC beta-lactamase family. {ECO:0000256|ARBA:ARBA00005250}.
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DR EMBL; CP000555; ABM95145.1; -; Genomic_DNA.
DR RefSeq; WP_011829782.1; NC_008825.1.
DR AlphaFoldDB; A2SHV6; -.
DR STRING; 420662.Mpe_A2189; -.
DR KEGG; mpt:Mpe_A2189; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_056342_0_2_4; -.
DR Proteomes; UP000000366; Chromosome.
DR CDD; cd16282; metallo-hydrolase-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR42951:SF20; BETA LACTAMASE; 1.
DR PANTHER; PTHR42951; METALLO-BETA-LACTAMASE DOMAIN-CONTAINING; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..323
FT /note="Metallo-beta-lactamase type 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002645822"
FT DOMAIN 65..250
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 323 AA; 34777 MW; B49877BF1FC1D450 CRC64;
MQFAIRRRIL LPLVGALGLA AASGCATLAA PGADPTAPRA VEVASGVYMV QGSSGEVDLA
NQGRLGNAGF IVGDAGVIAI DSGTSYRHGQ ALLAEIARVT DKPVKLLLLT HARQEFIFGA
AAFRERGIPV QMQRKASRLM TARCEGCLKT LNRVLGEEAM RGTVMFKPDT EFDAPYESGL
IGRPVRVLYY GHSSGPGDIA VLDGRTGVLF AGGLLDQRRI PDVQDGEIDG WRQALQALRG
LPIRQVVPGH GPVASAALID GVDRYLTQLE SRLIELTRAD AALSEVPDAA GLPEFKDWDQ
YQTIHRRNAS IVFVRMERDL LVR
//
