ID K2AD16_9BACT Unreviewed; 363 AA.
AC K2AD16;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=ACD_54C01323G0010 {ECO:0000313|EMBL:EKD59496.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD59496.1};
RN [1] {ECO:0000313|EMBL:EKD59496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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 -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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:EKD59496.1}.
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DR EMBL; AMFJ01024092; EKD59496.1; -; Genomic_DNA.
DR AlphaFoldDB; K2AD16; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}.
FT DOMAIN 143..333
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 363 AA; 40662 MW; E697D8171E8A3376 CRC64;
MDPVIAQEMM IFDMLPPNLP PPCHEARRFA RAAHMDDSAP SFLTHHILSL RKMEPAMFFS
QTPVWQSFGD RLVSTLTRRF AEQGLTRDSL GLVLVTPGTD GPEGFAHRGD WRCYPCSLVK
SFHLIHALAA LEEGRVVPHG DLDRALRDMV RWSSNTATNY AIDLITGTTG DTLLQGAEYL
DWVAKRERLN RFYWALGWPE WEGCTISQKL MDDTRYGREA QYAGVDGANL NALTPLAAAR
LLWELFQGTL PLSAPSKARA QAILRRDATG EDAANPHYQL AEYLGGDLPV GAELWSKAGH
NLWTGDARTS WFKHDMLRLL VPGRRPLIVA VMTQGQALAE THPQAFPAMG RLIWEMTEEM
TRA
//
